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Collagen alpha-5(IV) chain

 CO4A5_HUMAN             Reviewed;        1685 AA.
P29400; Q16006; Q16126; Q6LD84; Q7Z700; Q9NUB7;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
25-OCT-2017, entry version 204.
RecName: Full=Collagen alpha-5(IV) chain;
Flags: Precursor;
Name=COL4A5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8120014;
Zhou J., Leinonen A., Tryggvason K.;
"Structure of the human type IV collagen COL4A5 gene.";
J. Biol. Chem. 269:6608-6614(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE OF 1-910, AND VARIANT APSX CYS-521.
TISSUE=Kidney;
PubMed=1352287;
Zhou J., Hertz J.M., Leinonen A., Tryggvason K.;
"Complete amino acid sequence of the human alpha 5 (IV) collagen chain
and identification of a single-base mutation in exon 23 converting
glycine 521 in the collagenous domain to cysteine in an Alport
syndrome patient.";
J. Biol. Chem. 267:12475-12481(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 85-1685.
TISSUE=Placenta;
PubMed=2380186;
Pihlajaniemi T., Pohjolainen E.R., Myers J.C.;
"Complete primary structure of the triple-helical region and the
carboxyl-terminal domain of a new type IV collagen chain, alpha
5(IV).";
J. Biol. Chem. 265:13758-13766(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 924-1685.
PubMed=2004755; DOI=10.1016/0888-7543(91)90214-Y;
Zhou J., Hostikka S.L., Chow L.T., Tryggvason K.;
"Characterization of the 3' half of the human type IV collagen alpha 5
gene that is affected in the Alport syndrome.";
Genomics 9:1-9(1991).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 914-1685.
PubMed=1689491; DOI=10.1073/pnas.87.4.1606;
Hostikka S.L., Eddy R.L., Byers M.G., Hoeyhtyae M., Shows T.B.,
Tryggvason K.;
"Identification of a distinct type IV collagen alpha chain with
restricted kidney distribution and assignment of its gene to the locus
of X chromosome-linked Alport syndrome.";
Proc. Natl. Acad. Sci. U.S.A. 87:1606-1610(1990).
[8]
NUCLEOTIDE SEQUENCE OF 1442-1471.
PubMed=2339699;
Myers J.C., Jones T.A., Pohjolainen E.R., Kadri A.S., Goddard A.D.,
Sheer D., Solomon E., Pihlajaniemi T.;
"Molecular cloning of alpha 5(IV) collagen and assignment of the gene
to the region of the X chromosome containing the Alport syndrome
locus.";
Am. J. Hum. Genet. 46:1024-1033(1990).
[9]
NUCLEOTIDE SEQUENCE OF 1-20.
Guo C., van Damme B., Vanrenterghem Y., Devriendt K., Cassiman J.-J.,
Marynen P.;
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE OF 1258-1270 (ISOFORM 2).
PubMed=8301933; DOI=10.1038/ki.1993.384;
Guo C., van Damme B., van Damme-Lombaerts R., van den Berghe H.,
Cassiman J.-J., Marynen P.;
"Differential splicing of COL4A5 mRNA in kidney and white blood cells:
a complex mutation in the COL4A5 gene of an Alport patient deletes the
NC1 domain.";
Kidney Int. 44:1316-1321(1993).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1589-1598 AND 1677-1685, AND
VARIANTS APSX 1597-TYR--THR-1685 DEL AND 1679-GLQ--THR-1685 DEL.
PubMed=7853788; DOI=10.1038/ki.1994.399;
Nakazato H., Hattori S., Ushijima T., Matsuura T., Koitabashi Y.,
Takada T., Yoshioka K., Endo F., Matsuda I.;
"Mutations in the COL4A5 gene in Alport syndrome: a possible mutation
in primordial germ cells.";
Kidney Int. 46:1307-1314(1994).
[12]
REVIEW ON VARIANTS.
PubMed=9195222;
DOI=10.1002/(SICI)1098-1004(1997)9:6<477::AID-HUMU1>3.3.CO;2-H;
Lemmink H.H., Schroeder C.H., Monnens L.A.H., Smeets H.J.M.;
"The clinical spectrum of type IV collagen mutations.";
Hum. Mutat. 9:477-499(1997).
[13]
VARIANT APSX SER-1564.
PubMed=1672282; DOI=10.1016/0888-7543(91)90215-Z;
Zhou J., Barker D.F., Hostikka S.L., Gregory M.C., Atkin C.L.,
Tryggvason K.;
"Single base mutation in alpha 5(IV) collagen chain gene converting a
conserved cysteine to serine in Alport syndrome.";
Genomics 9:10-18(1991).
[14]
VARIANT APSX ARG-325.
PubMed=1376965;
Knebelmann B., Deschenes G., Gros F., Hors M.-C., Gruenfeld J.-P.,
Tryggvason K., Gubler M.-C., Antignac C.;
"Substitution of arginine for glycine 325 in the collagen alpha 5 (IV)
chain associated with X-linked Alport syndrome: characterization of
the mutation by direct sequencing of PCR-amplified lymphoblast cDNA
fragments.";
Am. J. Hum. Genet. 51:135-142(1992).
[15]
VARIANT APSX GLU-325.
PubMed=1363780; DOI=10.1093/hmg/1.2.127;
Renieri A., Seri M., Myers J.C., Pihlajaniemi T., Massella L.,
Rizzoni G.F., de Marchi M.;
"De novo mutation in the COL4A5 gene converting glycine 325 to
glutamic acid in Alport syndrome.";
Hum. Mol. Genet. 1:127-129(1992).
[16]
VARIANTS APSX THR-1517; SER-1538 AND GLN-1563.
PubMed=8406498; DOI=10.1006/geno.1993.1351;
Lemmink H.L., Schroeder C.H., Brunner H.G., Nelen M.R., Zhou J.,
Tryggvason K., Haggsma-Schouten W.A.G., Roodvoets A.P., Rascher W.,
van Oost B.A., Smeets H.J.M.;
"Identification of four novel mutations in the COL4A5 gene of patients
with Alport syndrome.";
Genomics 17:485-489(1993).
[17]
INVOLVEMENT IN DL-ATS.
PubMed=8356449; DOI=10.1126/science.8356449;
Zhou J., Mochizuki T., Smeets H., Antignac C., Laurila P.,
de Paepe A., Tryggvason K., Reeders S.T.;
"Deletion of the paired alpha 5(IV) and alpha 6(IV) collagen genes in
inherited smooth muscle tumors.";
Science 261:1167-1169(1993).
[18]
VARIANTS APSX GLU-400; VAL-406; VAL-638; ALA-638; ARG-653; ARG-796;
ARG-869; ARG-872 AND CYS-1241.
PubMed=7599631; DOI=10.1002/humu.1380050303;
Boye E., Flinter F., Zhou J., Tryggvason K., Bobrow M., Harris A.;
"Detection of 12 novel mutations in the collagenous domain of the
COL4A5 gene in Alport syndrome patients.";
Hum. Mutat. 5:197-204(1995).
[19]
VARIANT APSX ARG-1649.
PubMed=8651292;
Barker D.F., Pruchno C.J., Jiang X., Atkin C.L., Stone E.M.,
Denison J.C., Fain P.R., Gregory M.C.;
"A mutation causing Alport syndrome with tardive hearing loss is
common in the western United States.";
Am. J. Hum. Genet. 58:1157-1165(1996).
[20]
VARIANTS APSX.
PubMed=8651296;
Renieri A., Bruttini M., Galli L., Zanelli P., Neri T.M., Rossetti S.,
Turco A.E., Heiskari N., Zhou J., Gusmano R., Massella L., Banfi G.,
Scolari F., Sessa A., Rizzoni G.F., Tryggvason K., Pignatti P.F.,
Savi M., Ballabio A., de Marchi M.;
"X-linked Alport syndrome: an SSCP-based mutation survey over all 51
exons of the COL4A5 gene.";
Am. J. Hum. Genet. 58:1192-1204(1996).
[21]
VARIANTS APSX, AND VARIANTS ASP-430; SER-444; SER-619; ASN-664 AND
MET-1428.
PubMed=8940267;
Knebelmann B., Breillat C., Forestier L., Arrondel C., Jacassier D.,
Giatras I., Drouot L., Deschenes G., Gruenfeld J.-P., Broyer M.,
Gubler M.-C., Antignac C.;
"Spectrum of mutations in the COL4A5 collagen gene in X-linked Alport
syndrome.";
Am. J. Hum. Genet. 59:1221-1232(1996).
[22]
VARIANT APSX ASP-1498.
PubMed=8829632;
DOI=10.1002/(SICI)1098-1004(1996)7:2<149::AID-HUMU9>3.3.CO;2-A;
Tverskaya S., Bobrynina V., Tsalykova F., Ignatova M.,
Krasnopolskaya X., Evgrafov O.;
"Substitution of A1498D in noncollagen domain of a5(IV) collagen chain
associated with adult-onset X-linked Alport syndrome.";
Hum. Mutat. 7:149-150(1996).
[23]
VARIANT APSX GLN-1677.
PubMed=9150741; DOI=10.1007/s004390050429;
Barker D.F., Denison J.C., Atkin C.L., Gregory M.C.;
"Common ancestry of three Ashkenazi-American families with Alport
syndrome and COL4A5 R1677Q.";
Hum. Genet. 99:681-684(1997).
[24]
VARIANTS APSX ARG-174; ARG-177; ARG-325; CYS-1410; TRP-1421; THR-1517
AND ASP-1596.
PubMed=9452056;
Neri T.M., Zanelli P., de Palma G., Savi M., Rossetti S., Turco A.E.,
Pignatti G.F., Galli L., Bruttini M., Renieri A., Mingarelli R.,
Trivelli A., Pinciaroli A.R., Ragaiolo M., Rizzoni G.F., de Marchi M.;
"Missense mutations in the COL4A5 gene in patients with X-linked
Alport syndrome.";
Hum. Mutat. Suppl. 1:S106-S109(1998).
[25]
VARIANTS APSX VAL-420; 456-PRO--PRO-458 DEL; ASP-573; ASP-624;
ASP-635; 802-GLY--PRO-807 DEL; ARG-869; CYS-941; SER-1030; SER-1066;
ASP-1143; ARG-1196; GLU-1261; SER-1357 AND ARG-1649.
PubMed=9848783;
Martin P., Heiskari N., Zhou J., Leinonen A., Tumelius T., Hertz J.M.,
Barker D.F., Gregory M.C., Atkin C.L., Styrkarsdottir U., Neumann H.,
Springate J., Shows T.B., Pettersson E., Tryggvason K.;
"High mutation detection rate in the COL4A5 collagen gene in suspected
Alport syndrome using PCR and direct DNA sequencing.";
J. Am. Soc. Nephrol. 9:2291-2301(1998).
[26]
VARIANTS APSX GLU-579; LYS-633; ASP-947; VAL-953; ARG-1107; ARG-1158;
SER-1170 AND TRP-1678, AND VARIANTS SER-444 AND ALA-739.
PubMed=10561141; DOI=10.1016/S0272-6386(99)70042-9;
Inoue Y., Nishio H., Shirakawa T., Nakanishi K., Nakamura H.,
Sumino K., Nishiyama K., Iijima K., Yoshikawa N.;
"Detection of mutations in the COL4A5 gene in over 90% of male
patients with X-linked Alport's syndrome by RT-PCR and direct
sequencing.";
Am. J. Kidney Dis. 34:854-862(1999).
[27]
VARIANT APSX ARG-822.
PubMed=10563487; DOI=10.1034/j.1399-0004.1999.560312.x;
Cruz-Robles D., Garcia-Torres R., Antignac C., Forestier L.,
Garcia de la Puente S., Correa-Rotter R., Garcia-Lopez E., Orozco L.;
"Three novel mutations in the COL4A5 gene in Mexican Alport syndrome
patients.";
Clin. Genet. 56:242-243(1999).
[28]
VARIANTS APSX, AND VARIANTS.
PubMed=10094548;
DOI=10.1002/(SICI)1098-1004(1999)13:2<124::AID-HUMU4>3.0.CO;2-Z;
Plant K.E., Green P.M., Vetrie D., Flinter F.A.;
"Detection of mutations in COL4A5 in patients with Alport syndrome.";
Hum. Mutat. 13:124-132(1999).
[29]
VARIANT APSX CYS-177.
PubMed=11004279; DOI=10.1016/S0002-9394(00)00466-9;
Blasi M.A., Rinaldi R., Renieri A., Petrucci R., De Bernardo C.,
Bruttini M., Grammatico P.;
"Dot-and-fleck retinopathy in Alport syndrome caused by a novel
mutation in the COL4A5 gene.";
Am. J. Ophthalmol. 130:130-131(2000).
[30]
VARIANTS APSX ARG-216; ARG-415; GLU-1045; ASP-1086; SER-1167 AND
864-SER--GLY-875 DEL.
PubMed=10862091;
DOI=10.1002/1098-1004(200006)15:6<579::AID-HUMU13>3.3.CO;2-B;
Martin P., Heiskari N., Pajari H., Groenhagen-Riska C.,
Kaeaeriaeinen H., Koskimies O., Tryggvason K.;
"Spectrum of COL4A5 mutations in Finnish Alport syndrome patients.";
Hum. Mutat. 15:579-579(2000).
[31]
VARIANTS APSX ARG-319; SER-739; VAL-902; GLU-911; ASP-1229 AND
HIS-1511.
PubMed=10684360; DOI=10.1007/s004670050025;
Cheong H.I., Park H.W., Ha I.S., Choi Y.;
"Mutational analysis of COL4A5 gene in Korean Alport syndrome.";
Pediatr. Nephrol. 14:117-121(2000).
[32]
VARIANTS APSX ARG-192; ARG-292; ASP-295; ARG-325; ARG-558; VAL-603;
ASP-624; ASP-629; GLU-722; VAL-898; ALA-1006; VAL-1006; ASP-1244;
ARG-1649 AND PRO-1677, AND VARIANT SER-444.
PubMed=11223851;
DOI=10.1002/1096-8628(20010115)98:2<148::AID-AJMG1024>3.0.CO;2-W;
Barker D.F., Denison J.C., Atkin C.L., Gregory M.C.;
"Efficient detection of Alport syndrome COL4A5 mutations with
multiplex genomic PCR-SSCP.";
Am. J. Med. Genet. 98:148-160(2001).
[33]
INVOLVEMENT IN DL-ATS.
PubMed=12784310; DOI=10.1002/ajmg.a.20019;
Anker M.C., Arnemann J., Neumann K., Ahrens P., Schmidt H., Koenig R.;
"Alport syndrome with diffuse leiomyomatosis.";
Am. J. Med. Genet. A 119:381-385(2003).
[34]
VARIANT APSX GLU-123.
PubMed=24522658; DOI=10.1007/s11033-014-3227-1;
Guo Y., Yuan J., Liang H., Xiao J., Xu H., Yuan L., Gao K., Wu B.,
Tang Y., Li X., Deng H.;
"Identification of a novel COL4A5 mutation in a Chinese family with X-
linked Alport syndrome using exome sequencing.";
Mol. Biol. Rep. 41:3631-3635(2014).
-!- FUNCTION: Type IV collagen is the major structural component of
glomerular basement membranes (GBM), forming a 'chicken-wire'
meshwork together with laminins, proteoglycans and
entactin/nidogen.
-!- SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)-
alpha 6(IV), each of which can form a triple helix structure with
2 other chains to generate type IV collagen network.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P29400-1; Sequence=Displayed;
Name=2;
IsoId=P29400-2; Sequence=VSP_001173;
Note=Contains 2 extra G-X-X repeats into the triple-helix
domain.;
-!- TISSUE SPECIFICITY: Isoform 2 is found in kidney.
-!- DOMAIN: Alpha chains of type IV collagen have a non-collagenous
domain (NC1) at their C-terminus, frequent interruptions of the G-
X-Y repeats in the long central triple-helical domain (which may
cause flexibility in the triple helix), and a short N-terminal
triple-helical 7S domain.
-!- PTM: Prolines at the third position of the tripeptide repeating
unit (G-X-Y) are hydroxylated in some or all of the chains.
-!- PTM: Type IV collagens contain numerous cysteine residues which
are involved in inter- and intramolecular disulfide bonding. 12 of
these, located in the NC1 domain, are conserved in all known type
IV collagens.
-!- PTM: The trimeric structure of the NC1 domains is stabilized by
covalent bonds between Lys and Met residues. {ECO:0000250}.
-!- DISEASE: Alport syndrome, X-linked (APSX) [MIM:301050]: A syndrome
that is characterized by progressive glomerulonephritis, renal
failure, sensorineural deafness, specific eye abnormalities
(lenticonous and macular flecks), and glomerular basement membrane
defects. The disorder shows considerable heterogeneity in that
families differ in the age of end-stage renal disease and the
occurrence of deafness. {ECO:0000269|PubMed:10094548,
ECO:0000269|PubMed:10561141, ECO:0000269|PubMed:10563487,
ECO:0000269|PubMed:10684360, ECO:0000269|PubMed:10862091,
ECO:0000269|PubMed:11004279, ECO:0000269|PubMed:11223851,
ECO:0000269|PubMed:1352287, ECO:0000269|PubMed:1363780,
ECO:0000269|PubMed:1376965, ECO:0000269|PubMed:1672282,
ECO:0000269|PubMed:24522658, ECO:0000269|PubMed:7599631,
ECO:0000269|PubMed:7853788, ECO:0000269|PubMed:8406498,
ECO:0000269|PubMed:8651292, ECO:0000269|PubMed:8651296,
ECO:0000269|PubMed:8829632, ECO:0000269|PubMed:8940267,
ECO:0000269|PubMed:9150741, ECO:0000269|PubMed:9452056,
ECO:0000269|PubMed:9848783}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Deletions covering the N-terminal regions of COL4A5
and COL4A6, which are localized in a head-to-head manner, are
found in the chromosome Xq22.3 centromeric deletion syndrome. This
results in a phenotype with features of diffuse leiomyomatosis and
Alport syndrome (DL-ATS).
-!- SIMILARITY: Belongs to the type IV collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00736}.
-!- WEB RESOURCE: Name= Alport syndrome and COL4A5;
URL="http://www.arup.utah.edu/database/ALPORT/ALPORT_welcome.php";
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EMBL; M58526; AAA99480.1; -; mRNA.
EMBL; AL034369; CAA22267.2; -; Genomic_DNA.
EMBL; AL031622; CAA22267.2; JOINED; Genomic_DNA.
EMBL; AL035425; CAA22267.2; JOINED; Genomic_DNA.
EMBL; AL035425; CAB90289.2; -; Genomic_DNA.
EMBL; AL031622; CAB90289.2; JOINED; Genomic_DNA.
EMBL; AL034369; CAB90289.2; JOINED; Genomic_DNA.
EMBL; AL031622; CAI43038.1; -; Genomic_DNA.
EMBL; AL034369; CAI43038.1; JOINED; Genomic_DNA.
EMBL; AL035425; CAI43038.1; JOINED; Genomic_DNA.
EMBL; AL136364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471120; EAX02683.1; -; Genomic_DNA.
EMBL; M90464; AAA52046.1; -; mRNA.
EMBL; U04520; AAC27816.1; -; Genomic_DNA.
EMBL; U04470; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04471; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04472; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04473; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04474; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04476; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04477; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04478; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04479; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04480; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04483; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04485; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04486; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04487; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04488; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04489; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04490; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04491; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04492; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04493; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04494; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04495; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04496; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04497; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04498; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04499; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04500; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04501; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04502; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04503; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04504; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04505; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04506; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04507; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04508; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04509; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04510; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04511; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04512; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04514; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04515; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04516; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04517; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04518; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04519; AAC27816.1; JOINED; Genomic_DNA.
EMBL; U04520; AAF66217.2; -; Genomic_DNA.
EMBL; U04470; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04471; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04472; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04473; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04474; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04476; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04477; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04478; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04479; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04480; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04483; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04485; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04486; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04487; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04488; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04489; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04490; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04491; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04492; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04493; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04494; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04495; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04496; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04497; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04498; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04499; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04500; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04501; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04502; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04503; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04504; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04505; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04506; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04507; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04508; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04509; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04510; AAF66217.2; JOINED; Genomic_DNA.
EMBL; AF199451; AAF66217.2; JOINED; Genomic_DNA.
EMBL; AF199452; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04511; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04512; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04514; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04515; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04516; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04517; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04518; AAF66217.2; JOINED; Genomic_DNA.
EMBL; U04519; AAF66217.2; JOINED; Genomic_DNA.
EMBL; M63473; AAA51558.1; -; Genomic_DNA.
EMBL; M63455; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63456; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63457; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63458; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63459; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63460; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63461; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63462; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63463; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63464; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63465; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63466; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63467; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63468; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63470; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63471; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M63472; AAA51558.1; JOINED; Genomic_DNA.
EMBL; M31115; AAA52045.1; -; mRNA.
EMBL; Z37153; CAA85512.1; -; Genomic_DNA.
EMBL; S69168; AAC60612.1; -; mRNA.
EMBL; S59334; AAD13909.1; -; mRNA.
EMBL; S75903; AAB33374.1; -; Genomic_DNA.
CCDS; CCDS14543.1; -. [P29400-1]
CCDS; CCDS35366.1; -. [P29400-2]
PIR; S22917; S22917.
RefSeq; NP_000486.1; NM_000495.4. [P29400-1]
RefSeq; NP_203699.1; NM_033380.2. [P29400-2]
UniGene; Hs.369089; -.
ProteinModelPortal; P29400; -.
SMR; P29400; -.
BioGrid; 107684; 22.
IntAct; P29400; 19.
MINT; MINT-1388512; -.
STRING; 9606.ENSP00000331902; -.
ChEMBL; CHEMBL2364188; -.
iPTMnet; P29400; -.
PhosphoSitePlus; P29400; -.
BioMuta; COL4A5; -.
DMDM; 461675; -.
EPD; P29400; -.
MaxQB; P29400; -.
PeptideAtlas; P29400; -.
PRIDE; P29400; -.
Ensembl; ENST00000328300; ENSP00000331902; ENSG00000188153. [P29400-2]
Ensembl; ENST00000361603; ENSP00000354505; ENSG00000188153. [P29400-1]
GeneID; 1287; -.
KEGG; hsa:1287; -.
UCSC; uc004enz.3; human. [P29400-1]
CTD; 1287; -.
DisGeNET; 1287; -.
EuPathDB; HostDB:ENSG00000188153.12; -.
GeneCards; COL4A5; -.
GeneReviews; COL4A5; -.
H-InvDB; HIX0028371; -.
HGNC; HGNC:2207; COL4A5.
HPA; HPA065449; -.
MalaCards; COL4A5; -.
MIM; 301050; phenotype.
MIM; 303630; gene.
neXtProt; NX_P29400; -.
OpenTargets; ENSG00000188153; -.
Orphanet; 88917; X-linked Alport syndrome.
Orphanet; 1018; X-linked diffuse leiomyomatosis - Alport syndrome.
PharmGKB; PA26722; -.
GeneTree; ENSGT00900000140804; -.
HOGENOM; HOG000085652; -.
HOVERGEN; HBG004933; -.
InParanoid; P29400; -.
KO; K06237; -.
OMA; HCPQGWD; -.
OrthoDB; EOG091G0613; -.
TreeFam; TF344135; -.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474244; Extracellular matrix organization.
Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-HSA-186797; Signaling by PDGF.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-2214320; Anchoring fibril formation.
Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
Reactome; R-HSA-3000157; Laminin interactions.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-419037; NCAM1 interactions.
Reactome; R-HSA-8948216; Collagen chain trimerization.
GeneWiki; COL4A5; -.
GenomeRNAi; 1287; -.
PRO; PR:P29400; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000188153; -.
CleanEx; HS_COL4A5; -.
ExpressionAtlas; P29400; baseline and differential.
Genevisible; P29400; HS.
GO; GO:0005605; C:basal lamina; IEA:Ensembl.
GO; GO:0005587; C:collagen type IV trimer; TAS:ProtInc.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
Gene3D; 2.160.20.50; -; 6.
Gene3D; 2.170.240.10; -; 1.
InterPro; IPR008160; Collagen.
InterPro; IPR001442; Collagen_IV_NC.
InterPro; IPR036954; Collagen_IV_NC_sf.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR016133; Insect_cyst_antifreeze_prot.
Pfam; PF01413; C4; 2.
Pfam; PF01391; Collagen; 20.
SMART; SM00111; C4; 2.
SUPFAM; SSF56436; SSF56436; 2.
PROSITE; PS51403; NC1_IV; 1.
1: Evidence at protein level;
Alport syndrome; Alternative splicing; Basement membrane;
Chromosomal rearrangement; Collagen; Complete proteome; Deafness;
Disease mutation; Disulfide bond; Extracellular matrix; Glycoprotein;
Hydroxylation; Polymorphism; Reference proteome; Repeat; Secreted;
Signal.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 1685 Collagen alpha-5(IV) chain.
/FTId=PRO_0000005852.
DOMAIN 1461 1685 Collagen IV NC1. {ECO:0000255|PROSITE-
ProRule:PRU00736}.
REGION 27 41 Nonhelical region (NC2).
REGION 42 1456 Triple-helical region.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 451 451 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00736}.
DISULFID 481 481 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00736}.
DISULFID 484 484 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00736}.
DISULFID 1476 1567 Or C-1476 with C-1564.
{ECO:0000255|PROSITE-ProRule:PRU00736}.
DISULFID 1509 1564 Or C-1509 with C-1567.
{ECO:0000255|PROSITE-ProRule:PRU00736}.
DISULFID 1521 1527 {ECO:0000255|PROSITE-ProRule:PRU00736}.
DISULFID 1586 1681 Or C-1586 with C-1678.
{ECO:0000255|PROSITE-ProRule:PRU00736}.
DISULFID 1620 1678 Or C-1620 with C-1681.
{ECO:0000255|PROSITE-ProRule:PRU00736}.
DISULFID 1632 1638 {ECO:0000255|PROSITE-ProRule:PRU00736}.
CROSSLNK 1549 1549 S-Lysyl-methionine sulfilimine (Met-Lys)
(interchain with K-1667). {ECO:0000250}.
CROSSLNK 1667 1667 S-Lysyl-methionine sulfilimine (Lys-Met)
(interchain with M-1549). {ECO:0000250}.
VAR_SEQ 1264 1264 G -> GPTGFQG (in isoform 2).
{ECO:0000305}.
/FTId=VSP_001173.
VARIANT 54 54 G -> D (in APSX; adult type;
dbSNP:rs104886043).
/FTId=VAR_001914.
VARIANT 114 114 G -> S (in APSX).
/FTId=VAR_007991.
VARIANT 123 123 G -> E (in APSX).
{ECO:0000269|PubMed:24522658}.
/FTId=VAR_071932.
VARIANT 129 129 G -> E (in APSX; juvenile type;
dbSNP:rs281874723).
/FTId=VAR_001915.
VARIANT 129 129 G -> V (in APSX; juvenile type;
dbSNP:rs281874723).
/FTId=VAR_001916.
VARIANT 174 174 G -> R (in APSX; dbSNP:rs104886055).
{ECO:0000269|PubMed:9452056}.
/FTId=VAR_001917.
VARIANT 177 177 G -> C (in APSX; presenting with dot-and-
fleck retinopathy; dbSNP:rs104886056).
{ECO:0000269|PubMed:11004279}.
/FTId=VAR_011220.
VARIANT 177 177 G -> R (in APSX; adult type;
dbSNP:rs104886056).
{ECO:0000269|PubMed:9452056}.
/FTId=VAR_001918.
VARIANT 192 192 G -> R (in APSX; dbSNP:rs104886060).
{ECO:0000269|PubMed:11223851}.
/FTId=VAR_011221.
VARIANT 204 204 G -> V (in APSX; juvenile type;
dbSNP:rs104886063).
/FTId=VAR_011222.
VARIANT 216 216 G -> R (in APSX; juvenile type;
dbSNP:rs104886067).
{ECO:0000269|PubMed:10862091}.
/FTId=VAR_001919.
VARIANT 219 219 G -> S (in APSX; dbSNP:rs104886075).
/FTId=VAR_001920.
VARIANT 230 230 G -> R (in APSX; juvenile type;
dbSNP:rs104886076).
/FTId=VAR_011223.
VARIANT 239 239 G -> E (in APSX; dbSNP:rs104886068).
/FTId=VAR_011224.
VARIANT 264 264 G -> R (in APSX; adult type;
dbSNP:rs104886069).
/FTId=VAR_011225.
VARIANT 289 289 G -> V (in APSX; juvenile type;
dbSNP:rs104886450).
/FTId=VAR_001921.
VARIANT 292 292 G -> R (in APSX; dbSNP:rs104886073).
{ECO:0000269|PubMed:11223851}.
/FTId=VAR_011226.
VARIANT 292 292 G -> V (in APSX; juvenile type;
dbSNP:rs104886078).
/FTId=VAR_001922.
VARIANT 295 295 G -> D (in APSX; dbSNP:rs104886079).
{ECO:0000269|PubMed:11223851}.
/FTId=VAR_011227.
VARIANT 298 298 G -> S (in APSX; dbSNP:rs104886080).
/FTId=VAR_011228.
VARIANT 319 319 G -> R (in APSX; juvenile type;
dbSNP:rs104886085).
{ECO:0000269|PubMed:10684360}.
/FTId=VAR_011229.
VARIANT 325 325 G -> E (in APSX; dbSNP:rs104886091).
{ECO:0000269|PubMed:1363780}.
/FTId=VAR_001923.
VARIANT 325 325 G -> R (in APSX; juvenile and adult
types; dbSNP:rs104886088).
{ECO:0000269|PubMed:11223851,
ECO:0000269|PubMed:1376965,
ECO:0000269|PubMed:9452056}.
/FTId=VAR_001924.
VARIANT 331 331 G -> V (in APSX; dbSNP:rs104886092).
/FTId=VAR_007992.
VARIANT 365 367 Missing (in APSX; juvenile type).
/FTId=VAR_001926.
VARIANT 365 365 G -> E (in APSX; juvenile type;
dbSNP:rs104886096).
/FTId=VAR_001925.
VARIANT 371 371 G -> E (in APSX; juvenile type;
dbSNP:rs104886097).
/FTId=VAR_001927.
VARIANT 374 374 G -> A (in APSX; dbSNP:rs104886108).
/FTId=VAR_001928.
VARIANT 383 383 G -> D (in APSX; juvenile type;
dbSNP:rs104886105).
/FTId=VAR_001929.
VARIANT 400 400 G -> E (in APSX; adult type;
dbSNP:rs104886107).
{ECO:0000269|PubMed:7599631}.
/FTId=VAR_001930.
VARIANT 406 406 G -> V (in APSX; adult type;
dbSNP:rs104886100).
{ECO:0000269|PubMed:7599631}.
/FTId=VAR_001931.
VARIANT 409 409 G -> D (in APSX; dbSNP:rs104886101).
/FTId=VAR_001932.
VARIANT 412 412 G -> V (in APSX; adult type;
dbSNP:rs104886102).
/FTId=VAR_011230.
VARIANT 415 415 G -> R (in APSX; dbSNP:rs104886103).
{ECO:0000269|PubMed:10862091}.
/FTId=VAR_011231.
VARIANT 420 420 G -> E (in APSX; juvenile type;
dbSNP:rs281874663).
/FTId=VAR_011232.
VARIANT 420 420 G -> V (in APSX).
{ECO:0000269|PubMed:9848783}.
/FTId=VAR_011233.
VARIANT 423 423 G -> E (in APSX; dbSNP:rs104886110).
/FTId=VAR_011234.
VARIANT 430 430 A -> D (in dbSNP:rs142883891).
{ECO:0000269|PubMed:8940267}.
/FTId=VAR_001933.
VARIANT 444 444 I -> S (in dbSNP:rs2272946).
{ECO:0000269|PubMed:10561141,
ECO:0000269|PubMed:11223851,
ECO:0000269|PubMed:8940267}.
/FTId=VAR_001934.
VARIANT 456 458 Missing (in APSX).
{ECO:0000269|PubMed:9848783}.
/FTId=VAR_001935.
VARIANT 466 466 G -> E (in APSX; dbSNP:rs104886114).
/FTId=VAR_001936.
VARIANT 472 472 G -> R (in APSX; dbSNP:rs104886116).
/FTId=VAR_007993.
VARIANT 491 491 G -> E (in APSX; juvenile type;
dbSNP:rs104886117).
/FTId=VAR_011235.
VARIANT 494 494 G -> D (in APSX; adult type;
dbSNP:rs104886118).
/FTId=VAR_001937.
VARIANT 496 507 Missing (in APSX; juvenile type).
/FTId=VAR_001938.
VARIANT 497 497 G -> C (in APSX; adult type;
dbSNP:rs104886120).
/FTId=VAR_011236.
VARIANT 521 521 G -> C (in APSX; dbSNP:rs104886121).
{ECO:0000269|PubMed:1352287}.
/FTId=VAR_001939.
VARIANT 521 521 G -> S (in APSX; dbSNP:rs104886121).
/FTId=VAR_001940.
VARIANT 524 524 G -> D (in APSX; adult type;
dbSNP:rs104886119).
/FTId=VAR_011237.
VARIANT 545 545 G -> R (in APSX; dbSNP:rs104886126).
/FTId=VAR_007994.
VARIANT 545 545 G -> V (in APSX; dbSNP:rs104886127).
/FTId=VAR_007995.
VARIANT 558 558 G -> R (in APSX; dbSNP:rs104886129).
{ECO:0000269|PubMed:11223851}.
/FTId=VAR_011238.
VARIANT 561 561 G -> R (in APSX; dbSNP:rs104886136).
/FTId=VAR_007996.
VARIANT 567 567 G -> A (in APSX; juvenile type;
dbSNP:rs104886137).
/FTId=VAR_001941.
VARIANT 573 573 G -> D (in APSX; dbSNP:rs104886138).
{ECO:0000269|PubMed:9848783}.
/FTId=VAR_011239.
VARIANT 579 579 G -> E (in APSX; dbSNP:rs104886130).
{ECO:0000269|PubMed:10561141}.
/FTId=VAR_011240.
VARIANT 579 579 G -> R (in APSX; adult type;
dbSNP:rs104886139).
/FTId=VAR_007997.
VARIANT 603 603 G -> V (in APSX; dbSNP:rs104886133).
{ECO:0000269|PubMed:11223851}.
/FTId=VAR_011241.
VARIANT 609 609 G -> R (in APSX; juvenile type;
dbSNP:rs104886135).
/FTId=VAR_011242.
VARIANT 609 609 G -> V (in APSX; juvenile type;
dbSNP:rs104886140).
/FTId=VAR_001942.
VARIANT 619 619 P -> S. {ECO:0000269|PubMed:8940267}.
/FTId=VAR_011243.
VARIANT 621 621 G -> C (in APSX; dbSNP:rs104886141).
/FTId=VAR_011244.
VARIANT 624 624 G -> D (in APSX; dbSNP:rs104886142).
{ECO:0000269|PubMed:11223851,
ECO:0000269|PubMed:9848783}.
/FTId=VAR_011245.
VARIANT 629 629 G -> D (in APSX; dbSNP:rs104886144).
{ECO:0000269|PubMed:11223851}.
/FTId=VAR_011246.
VARIANT 632 632 G -> D (in APSX; dbSNP:rs104886145).
/FTId=VAR_011247.
VARIANT 633 633 E -> K (in APSX; dbSNP:rs104886146).
{ECO:0000269|PubMed:10561141}.
/FTId=VAR_011248.
VARIANT 635 635 G -> D (in APSX; dbSNP:rs281874683).
{ECO:0000269|PubMed:9848783}.
/FTId=VAR_007998.
VARIANT 638 638 G -> A (in APSX; dbSNP:rs104886134).
{ECO:0000269|PubMed:7599631}.
/FTId=VAR_001944.
VARIANT 638 638 G -> S (in APSX; juvenile type;
dbSNP:rs104886147).
/FTId=VAR_007999.
VARIANT 638 638 G -> V (in APSX; dbSNP:rs104886134).
{ECO:0000269|PubMed:7599631}.
/FTId=VAR_001943.
VARIANT 653 653 G -> R (in APSX; juvenile type;
dbSNP:rs104886150).
{ECO:0000269|PubMed:7599631}.
/FTId=VAR_001945.
VARIANT 664 664 K -> N (in dbSNP:rs34077552).
{ECO:0000269|PubMed:8940267}.
/FTId=VAR_001946.
VARIANT 669 669 G -> A (in APSX; juvenile type;
dbSNP:rs104886151).
/FTId=VAR_008000.
VARIANT 681 681 G -> D (in APSX; dbSNP:rs104886158).
/FTId=VAR_011249.
VARIANT 684 684 G -> V (in APSX; adult type;
dbSNP:rs104886160).
/FTId=VAR_001947.
VARIANT 687 687 G -> E (in APSX; dbSNP:rs104886168).
/FTId=VAR_008001.
VARIANT 722 722 G -> E (in APSX; dbSNP:rs104886163).
{ECO:0000269|PubMed:11223851}.
/FTId=VAR_011250.
VARIANT 739 739 P -> A (in dbSNP:rs104886164).
{ECO:0000269|PubMed:10561141}.
/FTId=VAR_011251.
VARIANT 739 739 P -> S (in APSX; juvenile type;
dbSNP:rs104886164).
{ECO:0000269|PubMed:10684360}.
/FTId=VAR_011252.
VARIANT 740 740 G -> E (in APSX; juvenile type;
dbSNP:rs104886165).
/FTId=VAR_001948.
VARIANT 743 743 G -> D (in APSX; dbSNP:rs104886166).
/FTId=VAR_008002.
VARIANT 772 772 G -> D (in APSX; juvenile type;
dbSNP:rs104886173).
/FTId=VAR_001949.
VARIANT 796 796 G -> R (in APSX; dbSNP:rs104886177).
{ECO:0000269|PubMed:7599631}.
/FTId=VAR_001950.
VARIANT 802 807 Missing (in APSX).
{ECO:0000269|PubMed:9848783}.
/FTId=VAR_011254.
VARIANT 802 802 G -> R (in APSX; dbSNP:rs104886179).
/FTId=VAR_011253.
VARIANT 808 808 G -> E (in APSX; adult type;
dbSNP:rs104886180).
/FTId=VAR_008003.
VARIANT 811 811 G -> V (in APSX; juvenile type;
dbSNP:rs104886183).
/FTId=VAR_011255.
VARIANT 822 824 Missing (in APSX).
/FTId=VAR_008004.
VARIANT 822 822 G -> R (in APSX; dbSNP:rs104886184).
{ECO:0000269|PubMed:10563487}.
/FTId=VAR_011256.
VARIANT 852 852 G -> E (in APSX; juvenile type;
dbSNP:rs104886187).
/FTId=VAR_008005.
VARIANT 852 852 G -> R (in APSX; dbSNP:rs104886186).
/FTId=VAR_001951.
VARIANT 864 875 Missing (in APSX).
{ECO:0000269|PubMed:10862091}.
/FTId=VAR_011257.
VARIANT 866 866 G -> E (in APSX; adult type;
dbSNP:rs104886188).
/FTId=VAR_001952.
VARIANT 869 869 G -> R (in APSX; juvenile type;
dbSNP:rs104886189).
{ECO:0000269|PubMed:7599631,
ECO:0000269|PubMed:9848783}.
/FTId=VAR_001953.
VARIANT 872 872 G -> R (in APSX; dbSNP:rs104886190).
{ECO:0000269|PubMed:7599631}.
/FTId=VAR_001954.
VARIANT 878 878 G -> R (in APSX).
/FTId=VAR_008006.
VARIANT 898 898 M -> V (in APSX; mild phenotype;
dbSNP:rs104886192).
{ECO:0000269|PubMed:11223851}.
/FTId=VAR_011258.
VARIANT 902 902 G -> V (in APSX; juvenile type).
{ECO:0000269|PubMed:10684360}.
/FTId=VAR_011259.
VARIANT 911 911 G -> E (in APSX; dbSNP:rs104886363).
{ECO:0000269|PubMed:10684360}.
/FTId=VAR_011260.
VARIANT 941 941 G -> C (in APSX; dbSNP:rs104886196).
{ECO:0000269|PubMed:9848783}.
/FTId=VAR_011261.
VARIANT 942 942 Missing (in APSX).
/FTId=VAR_001955.
VARIANT 947 947 G -> D (in APSX; dbSNP:rs104886370).
{ECO:0000269|PubMed:10561141}.
/FTId=VAR_011262.
VARIANT 953 953 G -> V (in APSX; found on the same allele
as variant Glu-1211; dbSNP:rs78972735).
{ECO:0000269|PubMed:10561141}.
/FTId=VAR_011263.
VARIANT 988 992 Missing (in APSX; adult type).
/FTId=VAR_008007.
VARIANT 1006 1006 G -> A (in APSX).
{ECO:0000269|PubMed:11223851}.
/FTId=VAR_011264.
VARIANT 1006 1006 G -> V (in APSX; dbSNP:rs104886202).
{ECO:0000269|PubMed:11223851}.
/FTId=VAR_011265.
VARIANT 1015 1015 G -> E (in APSX).
/FTId=VAR_011266.
VARIANT 1015 1015 G -> V (in APSX; dbSNP:rs104886211).
/FTId=VAR_011267.
VARIANT 1030 1030 G -> S (in APSX; dbSNP:rs104886210).
{ECO:0000269|PubMed:9848783}.
/FTId=VAR_011268.
VARIANT 1036 1036 G -> V (in APSX; dbSNP:rs104886212).
/FTId=VAR_011269.
VARIANT 1039 1039 G -> S (in APSX; juvenile type;
dbSNP:rs104886214).
/FTId=VAR_011270.
VARIANT 1045 1045 G -> E (in APSX; dbSNP:rs104886215).
{ECO:0000269|PubMed:10862091}.
/FTId=VAR_011271.
VARIANT 1066 1066 G -> R (in APSX; dbSNP:rs104886219).
/FTId=VAR_011272.
VARIANT 1066 1066 G -> S (in APSX; dbSNP:rs104886219).
{ECO:0000269|PubMed:9848783}.
/FTId=VAR_011273.
VARIANT 1086 1086 G -> D (in APSX; dbSNP:rs104886232).
{ECO:0000269|PubMed:10862091}.
/FTId=VAR_011274.
VARIANT 1104 1104 G -> V (in APSX; dbSNP:rs104886224).
/FTId=VAR_001956.
VARIANT 1107 1107 G -> R (in APSX; dbSNP:rs104886225).
{ECO:0000269|PubMed:10561141}.
/FTId=VAR_008008.
VARIANT 1143 1143 G -> D (in APSX; juvenile type;
dbSNP:rs104886229).
{ECO:0000269|PubMed:9848783}.
/FTId=VAR_001957.
VARIANT 1143 1143 G -> S (in APSX; adult type;
dbSNP:rs104886228).
/FTId=VAR_001958.
VARIANT 1158 1158 G -> R (in APSX).
{ECO:0000269|PubMed:10561141}.
/FTId=VAR_011275.
VARIANT 1161 1161 G -> R (in APSX; dbSNP:rs104886235).
/FTId=VAR_008009.
VARIANT 1167 1167 G -> S (in APSX; dbSNP:rs104886236).
{ECO:0000269|PubMed:10862091}.
/FTId=VAR_011276.
VARIANT 1170 1170 G -> S (in APSX; dbSNP:rs104886237).
{ECO:0000269|PubMed:10561141}.
/FTId=VAR_011277.
VARIANT 1182 1182 G -> R (in APSX; juvenile type;
dbSNP:rs104886242).
/FTId=VAR_001959.
VARIANT 1196 1196 G -> R (in APSX; dbSNP:rs104886244).
{ECO:0000269|PubMed:9848783}.
/FTId=VAR_011278.
VARIANT 1205 1205 G -> C (in APSX; juvenile type;
dbSNP:rs104886245).
/FTId=VAR_011279.
VARIANT 1211 1211 G -> E (in APSX; found on the same allele
as variant Val-953; dbSNP:rs104886247).
/FTId=VAR_011280.
VARIANT 1211 1211 G -> R (in APSX; dbSNP:rs104886246).
/FTId=VAR_008010.
VARIANT 1220 1220 G -> D (in APSX; dbSNP:rs104886251).
/FTId=VAR_008011.
VARIANT 1229 1229 G -> D (in APSX; adult type;
dbSNP:rs104886253).
{ECO:0000269|PubMed:10684360}.
/FTId=VAR_011281.
VARIANT 1241 1241 G -> C (in APSX; dbSNP:rs104886255).
{ECO:0000269|PubMed:7599631}.
/FTId=VAR_001960.
VARIANT 1244 1244 G -> D (in APSX; dbSNP:rs104886261).
{ECO:0000269|PubMed:11223851}.
/FTId=VAR_011282.
VARIANT 1252 1252 G -> S (in APSX; adult type;
dbSNP:rs104886262).
/FTId=VAR_011283.
VARIANT 1261 1261 G -> E (in APSX; dbSNP:rs104886264).
{ECO:0000269|PubMed:9848783}.
/FTId=VAR_011284.
VARIANT 1270 1270 G -> S (in APSX; dbSNP:rs104886257).
/FTId=VAR_001961.
VARIANT 1333 1333 G -> S (in APSX; dbSNP:rs104886266).
/FTId=VAR_008012.
VARIANT 1357 1357 G -> S (in APSX; dbSNP:rs104886267).
{ECO:0000269|PubMed:9848783}.
/FTId=VAR_011285.
VARIANT 1379 1379 G -> V (in APSX; adult type;
dbSNP:rs104886269).
/FTId=VAR_001962.
VARIANT 1410 1410 R -> C (in APSX; adult and juvenile
types; dbSNP:rs104886270).
{ECO:0000269|PubMed:9452056}.
/FTId=VAR_001963.
VARIANT 1421 1421 G -> W (in APSX; adult type;
dbSNP:rs104886272).
{ECO:0000269|PubMed:9452056}.
/FTId=VAR_001964.
VARIANT 1422 1422 R -> C (in APSX; juvenile type;
dbSNP:rs144282156).
/FTId=VAR_001965.
VARIANT 1427 1427 G -> V (in APSX; adult type;
dbSNP:rs104886274).
/FTId=VAR_008013.
VARIANT 1428 1428 L -> M. {ECO:0000269|PubMed:8940267}.
/FTId=VAR_011286.
VARIANT 1442 1442 G -> D (in APSX; dbSNP:rs104886277).
/FTId=VAR_008014.
VARIANT 1451 1451 G -> S (in APSX; dbSNP:rs104886280).
/FTId=VAR_001966.
VARIANT 1486 1486 G -> A (in APSX; adult type;
dbSNP:rs104886282).
/FTId=VAR_008015.
VARIANT 1488 1488 S -> F (in APSX; dbSNP:rs104886283).
/FTId=VAR_011287.
VARIANT 1498 1498 A -> D (in APSX; dbSNP:rs104886284).
{ECO:0000269|PubMed:8829632}.
/FTId=VAR_001967.
VARIANT 1511 1511 R -> H (in APSX; juvenile type; could be
a non pathogenic variant;
dbSNP:rs104886285).
{ECO:0000269|PubMed:10684360}.
/FTId=VAR_011288.
VARIANT 1517 1517 P -> T (in APSX; juvenile type;
dbSNP:rs201220208).
{ECO:0000269|PubMed:8406498,
ECO:0000269|PubMed:9452056}.
/FTId=VAR_001968.
VARIANT 1538 1538 W -> S (in APSX; adult type;
dbSNP:rs104886293).
{ECO:0000269|PubMed:8406498}.
/FTId=VAR_001969.
VARIANT 1559 1559 P -> A (in dbSNP:rs104886295).
/FTId=VAR_008016.
VARIANT 1563 1563 R -> Q (in APSX; dbSNP:rs281874743).
{ECO:0000269|PubMed:8406498}.
/FTId=VAR_001970.
VARIANT 1564 1564 C -> S (in APSX; adult type;
dbSNP:rs104886287).
{ECO:0000269|PubMed:1672282}.
/FTId=VAR_001971.
VARIANT 1567 1567 C -> R (in APSX; juvenile type;
dbSNP:rs104886288).
/FTId=VAR_011289.
VARIANT 1596 1596 G -> D (in APSX; dbSNP:rs104886297).
{ECO:0000269|PubMed:9452056}.
/FTId=VAR_001972.
VARIANT 1597 1685 Missing (in APSX).
{ECO:0000269|PubMed:7853788}.
/FTId=VAR_019594.
VARIANT 1649 1649 L -> R (in APSX; adult type;
dbSNP:rs104886303).
{ECO:0000269|PubMed:11223851,
ECO:0000269|PubMed:8651292,
ECO:0000269|PubMed:9848783}.
/FTId=VAR_001973.
VARIANT 1677 1677 R -> P (in APSX; dbSNP:rs104886308).
{ECO:0000269|PubMed:11223851}.
/FTId=VAR_011290.
VARIANT 1677 1677 R -> Q (in APSX; dbSNP:rs104886308).
{ECO:0000269|PubMed:9150741}.
/FTId=VAR_001974.
VARIANT 1678 1678 C -> W (in APSX; dbSNP:rs104886311).
{ECO:0000269|PubMed:10561141}.
/FTId=VAR_011291.
VARIANT 1679 1685 Missing (in APSX).
/FTId=VAR_019595.
CONFLICT 440 441 AG -> GS (in Ref. 5; AAA99480).
{ECO:0000305}.
CONFLICT 625 628 FGPP -> LALQ (in Ref. 5; AAA99480).
{ECO:0000305}.
CONFLICT 667 668 LP -> FR (in Ref. 5; AAA99480).
{ECO:0000305}.
CONFLICT 888 888 A -> R (in Ref. 5; AAA99480).
{ECO:0000305}.
SEQUENCE 1685 AA; 161044 MW; 4450A6762F12A626 CRC64;
MKLRGVSLAA GLFLLALSLW GQPAEAAACY GCSPGSKCDC SGIKGEKGER GFPGLEGHPG
LPGFPGPEGP PGPRGQKGDD GIPGPPGPKG IRGPPGLPGF PGTPGLPGMP GHDGAPGPQG
IPGCNGTKGE RGFPGSPGFP GLQGPPGPPG IPGMKGEPGS IIMSSLPGPK GNPGYPGPPG
IQGLPGPTGI PGPIGPPGPP GLMGPPGPPG LPGPKGNMGL NFQGPKGEKG EQGLQGPPGP
PGQISEQKRP IDVEFQKGDQ GLPGDRGPPG PPGIRGPPGP PGGEKGEKGE QGEPGKRGKP
GKDGENGQPG IPGLPGDPGY PGEPGRDGEK GQKGDTGPPG PPGLVIPRPG TGITIGEKGN
IGLPGLPGEK GERGFPGIQG PPGLPGPPGA AVMGPPGPPG FPGERGQKGD EGPPGISIPG
PPGLDGQPGA PGLPGPPGPA GPHIPPSDEI CEPGPPGPPG SPGDKGLQGE QGVKGDKGDT
CFNCIGTGIS GPPGQPGLPG LPGPPGSLGF PGQKGEKGQA GATGPKGLPG IPGAPGAPGF
PGSKGEPGDI LTFPGMKGDK GELGSPGAPG LPGLPGTPGQ DGLPGLPGPK GEPGGITFKG
ERGPPGNPGL PGLPGNIGPM GPPGFGPPGP VGEKGIQGVA GNPGQPGIPG PKGDPGQTIT
QPGKPGLPGN PGRDGDVGLP GDPGLPGQPG LPGIPGSKGE PGIPGIGLPG PPGPKGFPGI
PGPPGAPGTP GRIGLEGPPG PPGFPGPKGE PGFALPGPPG PPGLPGFKGA LGPKGDRGFP
GPPGPPGRTG LDGLPGPKGD VGPNGQPGPM GPPGLPGIGV QGPPGPPGIP GPIGQPGLHG
IPGEKGDPGP PGLDVPGPPG ERGSPGIPGA PGPIGPPGSP GLPGKAGASG FPGTKGEMGM
MGPPGPPGPL GIPGRSGVPG LKGDDGLQGQ PGLPGPTGEK GSKGEPGLPG PPGPMDPNLL
GSKGEKGEPG LPGIPGVSGP KGYQGLPGDP GQPGLSGQPG LPGPPGPKGN PGLPGQPGLI
GPPGLKGTIG DMGFPGPQGV EGPPGPSGVP GQPGSPGLPG QKGDKGDPGI SSIGLPGLPG
PKGEPGLPGY PGNPGIKGSV GDPGLPGLPG TPGAKGQPGL PGFPGTPGPP GPKGISGPPG
NPGLPGEPGP VGGGGHPGQP GPPGEKGKPG QDGIPGPAGQ KGEPGQPGFG NPGPPGLPGL
SGQKGDGGLP GIPGNPGLPG PKGEPGFHGF PGVQGPPGPP GSPGPALEGP KGNPGPQGPP
GRPGLPGPEG PPGLPGNGGI KGEKGNPGQP GLPGLPGLKG DQGPPGLQGN PGRPGLNGMK
GDPGLPGVPG FPGMKGPSGV PGSAGPEGEP GLIGPPGPPG LPGPSGQSII IKGDAGPPGI
PGQPGLKGLP GPQGPQGLPG PTGPPGDPGR NGLPGFDGAG GRKGDPGLPG QPGTRGLDGP
PGPDGLQGPP GPPGTSSVAH GFLITRHSQT TDAPQCPQGT LQVYEGFSLL YVQGNKRAHG
QDLGTAGSCL RRFSTMPFMF CNINNVCNFA SRNDYSYWLS TPEPMPMSMQ PLKGQSIQPF
ISRCAVCEAP AVVIAVHSQT IQIPHCPQGW DSLWIGYSFM MHTSAGAEGS GQALASPGSC
LEEFRSAPFI ECHGRGTCNY YANSYSFWLA TVDVSDMFSK PQSETLKAGD LRTRISRCQV
CMKRT


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