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Collagen alpha-1(IV) chain [Cleaved into: Arresten]

 CO4A1_HUMAN             Reviewed;        1669 AA.
P02462; A7E2W4; B1AM70; Q1P9S9; Q5VWF6; Q86X41; Q8NF88; Q9NYC5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 3.
27-SEP-2017, entry version 194.
RecName: Full=Collagen alpha-1(IV) chain;
Contains:
RecName: Full=Arresten;
Flags: Precursor;
Name=COL4A1;
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], AND VARIANT PRO-555.
PubMed=2701944;
Soininen R., Huotari M., Ganguly A., Prockop D.J., Tryggvason K.;
"Structural organization of the gene for the alpha 1 chain of human
type IV collagen.";
J. Biol. Chem. 264:13565-13571(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
PRO-555 AND HIS-1334.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-943, AND VARIANT PRO-555.
TISSUE=Placenta;
PubMed=3311751; DOI=10.1111/j.1432-1033.1987.tb13450.x;
Brazel D., Oberbaeumer I., Dieringer H., Babel W., Glanville R.W.,
Deutzmann R., Kuehn K.;
"Completion of the amino acid sequence of the alpha 1 chain of human
basement membrane collagen (type IV) reveals 21 non-triplet
interruptions located within the collagenous domain.";
Eur. J. Biochem. 168:529-536(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
PubMed=3182844;
Soininen R., Huotari M., Hostikka S.L., Prockop D.J., Tryggvason K.;
"The structural genes for alpha 1 and alpha 2 chains of human type IV
collagen are divergently encoded on opposite DNA strands and have an
overlapping promoter region.";
J. Biol. Chem. 263:17217-17220(1988).
[6]
PROTEIN SEQUENCE OF 28-243.
PubMed=4043082; DOI=10.1111/j.1432-1033.1985.tb09186.x;
Glanville R.W., Qian R.Q., Siebold B., Risteli J., Kuehn K.;
"Amino acid sequence of the N-terminal aggregation and cross-linking
region (7S domain) of the alpha 1 (IV) chain of human basement
membrane collagen.";
Eur. J. Biochem. 152:213-219(1985).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 46-1257, AND VARIANT PRO-555.
TISSUE=Placenta;
PubMed=3691802; DOI=10.1016/0014-5793(87)81155-9;
Soininen R., Haka-Risku T., Prockop D.J., Tryggvason K.;
"Complete primary structure of the alpha 1-chain of human basement
membrane (type IV) collagen.";
FEBS Lett. 225:188-194(1987).
[8]
PROTEIN SEQUENCE OF 534-1447.
PubMed=6434307; DOI=10.1111/j.1432-1033.1984.tb08404.x;
Babel W., Glanville R.W.;
"Structure of human-basement-membrane (type IV) collagen. Complete
amino-acid sequence of a 914-residue-long pepsin fragment from the
alpha 1(IV) chain.";
Eur. J. Biochem. 143:545-556(1984).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1256-1669.
PubMed=2581969;
Pihlajaniemi T., Tryggvason K., Myers J.C., Kurkinen M., Lebo R.,
Cheung M.-C., Prockop D.J., Boyd C.D.;
"cDNA clones coding for the pro-alpha1(IV) chain of human type IV
procollagen reveal an unusual homology of amino acid sequences in two
halves of the carboxyl-terminal domain.";
J. Biol. Chem. 260:7681-7687(1985).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1259-1669.
PubMed=2582422; DOI=10.1073/pnas.82.11.3649;
Brinker J.M., Gudas L.J., Loidl H.R., Wang S.-Y., Rosenbloom J.,
Kefalides N.A., Myers J.C.;
"Restricted homology between human alpha 1 type IV and other
procollagen chains.";
Proc. Natl. Acad. Sci. U.S.A. 82:3649-3653(1985).
[11]
PROTEIN SEQUENCE OF 1441-1669, AND DISULFIDE BONDS.
TISSUE=Placenta;
PubMed=2844531; DOI=10.1111/j.1432-1033.1988.tb14321.x;
Siebold B., Deutzmann R., Kuehn K.;
"The arrangement of intra- and intermolecular disulfide bonds in the
carboxyterminal, non-collagenous aggregation and cross-linking domain
of basement-membrane type IV collagen.";
Eur. J. Biochem. 176:617-624(1988).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669, FUNCTION OF ARRESTEN, AND
TISSUE SPECIFICITY.
PubMed=10811134;
Colorado P.C., Torre A., Kamphaus G., Maeshima Y., Hopfer H.,
Takahashi K., Volk R., Zamborsky E.D., Herman S., Sarkar P.K.,
Ericksen M.B., Dhanabal M., Simons M., Post M., Kufe D.W.,
Weichselbaum R.R., Sukhatme V.P., Kalluri R.;
"Anti-angiogenic cues from vascular basement membrane collagen.";
Cancer Res. 60:2520-2526(2000).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
Fu J., Bai X., Wang W., Ruan C.;
"Arresten, a collagen-derived inhibitor of angiogenesis.";
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
Peng X., Yin B., Yuan J., Qiang B.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
Zheng Q.C., Song Z.F., Zheng Y.W., Li Y.Q., Shu X.;
"Molecular cloning and sequencing of human arresten gene.";
Zhonghua Shi Yan Wai Ke Za Zhi 19:46-47(2002).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
He A.B.;
"Cloning and expression of arresten in Escherichia coli and Pachia
pastoris.";
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[17]
NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669, FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Placenta;
PubMed=16481288;
Zheng J.P., Tang H.Y., Chen X.J., Yu B.F., Xie J., Wu T.C.;
"Construction of recombinant plasmid and prokaryotic expression in E.
coli and biological activity analysis of human placenta arresten
gene.";
Hepatobiliary Pancreat. Dis. Int. 5:74-79(2006).
[18]
IDENTIFICATION OF RECEPTOR, AND FUNCTION OF ARRESTEN.
PubMed=16151532; DOI=10.1172/JCI24813;
Sudhakar A., Nyberg P., Keshamouni V.G., Mannam A.P., Li J.,
Sugimoto H., Cosgrove D., Kalluri R.;
"Human alpha1 type IV collagen NC1 domain exhibits distinct
antiangiogenic activity mediated by alpha1beta1 integrin.";
J. Clin. Invest. 115:2801-2810(2005).
[19]
IDENTIFICATION OF RECEPTOR, AND FUNCTION OF ARRESTEN.
PubMed=18775695; DOI=10.1016/j.yexcr.2008.08.011;
Nyberg P., Xie L., Sugimoto H., Colorado P., Sund M., Holthaus K.,
Sudhakar A., Salo T., Kalluri R.;
"Characterization of the anti-angiogenic properties of arresten, an
alpha1beta1 integrin-dependent collagen-derived tumor suppressor.";
Exp. Cell Res. 314:3292-3305(2008).
[20]
INVOLVEMENT IN ICH, VARIANTS ICH LEU-352 AND GLY-538, VARIANTS VAL-144
AND VAL-1531, AND CHARACTERIZATION OF VARIANTS ICH LEU-352 AND
GLY-538.
PubMed=22522439; DOI=10.1002/ana.22682;
Weng Y.C., Sonni A., Labelle-Dumais C., de Leau M., Kauffman W.B.,
Jeanne M., Biffi A., Greenberg S.M., Rosand J., Gould D.B.;
"COL4A1 mutations in patients with sporadic late-onset intracerebral
hemorrhage.";
Ann. Neurol. 71:470-477(2012).
[21]
INVOLVEMENT IN BSVD, AND VARIANTS BSVD ARG-755; ARG-773; ASP-882 AND
ARG-1266.
PubMed=22574627; DOI=10.1111/j.1469-8749.2011.04198.x;
Shah S., Ellard S., Kneen R., Lim M., Osborne N., Rankin J.,
Stoodley N., van der Knaap M., Whitney A., Jardine P.;
"Childhood presentation of COL4A1 mutations.";
Dev. Med. Child. Neurol. 54:569-574(2012).
[22]
INVOLVEMENT IN BSVD, AND VARIANT BSVD LYS-1627.
PubMed=23394911; DOI=10.1016/j.ajo.2012.11.028;
Rodahl E., Knappskog P.M., Majewski J., Johansson S., Telstad W.,
Krakenes J., Boman H.;
"Variants of anterior segment dysgenesis and cerebral involvement in a
large family with a novel COL4A1 mutation.";
Am. J. Ophthalmol. 155:946-953(2013).
[23]
INVOLVEMENT IN SCHZ, AND VARIANTS SCHZC ARG-655; ARG-870; SER-897;
SER-948; GLU-1041; GLU-1082; ARG-1326; ASP-1332 AND LYS-1615.
PubMed=23225343; DOI=10.1002/ana.23736;
Yoneda Y., Haginoya K., Kato M., Osaka H., Yokochi K., Arai H.,
Kakita A., Yamamoto T., Otsuki Y., Shimizu S., Wada T., Koyama N.,
Mino Y., Kondo N., Takahashi S., Hirabayashi S., Takanashi J.,
Okumura A., Kumagai T., Hirai S., Nabetani M., Saitoh S., Hattori A.,
Yamasaki M., Kumakura A., Sugo Y., Nishiyama K., Miyatake S.,
Tsurusaki Y., Doi H., Miyake N., Matsumoto N., Saitsu H.;
"Phenotypic spectrum of COL4A1 mutations: porencephaly to
schizencephaly.";
Ann. Neurol. 73:48-57(2013).
[24]
INVOLVEMENT IN RATOR, AND VARIANT RATOR ARG-510.
PubMed=25228067; DOI=10.1007/s00417-014-2800-6;
Zenteno J.C., Crespi J., Buentello-Volante B., Buil J.A.,
Bassaganyas F., Vela-Segarra J.I., Diaz-Cascajosa J., Marieges M.T.;
"Next generation sequencing uncovers a missense mutation in COL4A1 as
the cause of familial retinal arteriolar tortuosity.";
Graefes Arch. Clin. Exp. Ophthalmol. 252:1789-1794(2014).
[25]
INVOLVEMENT IN BSVD, AND VARIANTS BSVD ARG-708 AND ARG-773.
PubMed=24628545; DOI=10.1111/cge.12379;
Deml B., Reis L.M., Maheshwari M., Griffis C., Bick D., Semina E.V.;
"Whole exome analysis identifies dominant COL4A1 mutations in patients
with complex ocular phenotypes involving microphthalmia.";
Clin. Genet. 86:475-481(2014).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1441-1669, AND ADDITIONAL
INTERCHAIN LINKS.
PubMed=12011424; DOI=10.1073/pnas.062183499;
Than M.E., Henrich S., Huber R., Ries A., Mann K., Kuhn K., Timpl R.,
Bourenkov G.P., Bartunik H.D., Bode W.;
"The 1.9-A crystal structure of the noncollagenous (NC1) domain of
human placenta collagen IV shows stabilization via a novel type of
covalent Met-Lys cross-link.";
Proc. Natl. Acad. Sci. U.S.A. 99:6607-6612(2002).
[28]
VARIANTS POREN1 SER-749 AND ARG-1236.
PubMed=15905400; DOI=10.1126/science.1109418;
Gould D.B., Phalan F.C., Breedveld G.J., van Mil S.E., Smith R.S.,
Schimenti J.C., Aguglia U., van der Knaap M.S., Heutink P.,
John S.W.M.;
"Mutations in Col4a1 cause perinatal cerebral hemorrhage and
porencephaly.";
Science 308:1167-1171(2005).
[29]
VARIANTS POREN1 ASP-1130 AND ARG-1423.
PubMed=16107487; DOI=10.1136/jmg.2005.035584;
Breedveld G., de Coo I.F., Lequin M.H., Arts W.F.M., Heutink P.,
Gould D.B., John S.W.M., Oostra B., Mancini G.M.S.;
"Novel mutations in three families confirm a major role of COL4A1 in
hereditary porencephaly.";
J. Med. Genet. 43:490-495(2006).
[30]
VARIANT BSVD GLU-562.
PubMed=16598045; DOI=10.1056/NEJMoa053727;
Gould D.B., Phalan F.C., van Mil S.E., Sundberg J.P., Vahedi K.,
Massin P., Bousser M.G., Heutink P., Miner J.H., Tournier-Lasserve E.,
John S.W.M.;
"Role of COL4A1 in small-vessel disease and hemorrhagic stroke.";
N. Engl. J. Med. 354:1489-1496(2006).
[31]
VARIANT BSVD ASP-720.
PubMed=17696175; DOI=10.1002/ana.21191;
Sibon I., Coupry I., Menegon P., Bouchet J.P., Gorry P., Burgelin I.,
Calvas P., Orignac I., Dousset V., Lacombe D., Orgogozo J.M.,
Arveiler B., Goizet C.;
"COL4A1 mutation in Axenfeld-Rieger anomaly with leukoencephalopathy
and stroke.";
Ann. Neurol. 62:177-184(2007).
[32]
VARIANTS HANAC VAL-498; ARG-519 AND GLU-528.
PubMed=18160688; DOI=10.1056/NEJMoa071906;
Plaisier E., Gribouval O., Alamowitch S., Mougenot B., Prost C.,
Verpont M.C., Marro B., Desmettre T., Cohen S.Y., Roullet E.,
Dracon M., Fardeau M., Van Agtmael T., Kerjaschki D., Antignac C.,
Ronco P.;
"COL4A1 mutations and hereditary angiopathy, nephropathy, aneurysms,
and muscle cramps.";
N. Engl. J. Med. 357:2687-2695(2007).
[33]
INTERCHAIN SULFILIMINE BONDS.
PubMed=19729652; DOI=10.1126/science.1176811;
Vanacore R., Ham A.-J.L., Voehler M., Sanders C.R., Conrads T.P.,
Veenstra T.D., Sharpless K.B., Dawson P.E., Hudson B.G.;
"A sulfilimine bond identified in collagen IV.";
Science 325:1230-1234(2009).
[34]
VARIANT BSVD ARG-805.
PubMed=17379824; DOI=10.1161/STROKEAHA.106.475194;
Vahedi K., Kubis N., Boukobza M., Arnoult M., Massin P.,
Tournier-Lasserve E., Bousser M.G.;
"COL4A1 mutation in a patient with sporadic, recurrent intracerebral
hemorrhage.";
Stroke 38:1461-1464(2007).
[35]
VARIANT POREN1 ARG-1580.
PubMed=19194877; DOI=10.1002/ana.21525;
de Vries L.S., Koopman C., Groenendaal F., Van Schooneveld M.,
Verheijen F.W., Verbeek E., Witkamp T.D., van der Worp H.B.,
Mancini G.;
"COL4A1 mutation in two preterm siblings with antenatal onset of
parenchymal hemorrhage.";
Ann. Neurol. 65:12-18(2009).
[36]
VARIANTS HANAC ARG-498; ARG-510 AND LEU-525.
PubMed=20818663; DOI=10.1002/ajmg.a.33659;
Plaisier E., Chen Z., Gekeler F., Benhassine S., Dahan K., Marro B.,
Alamowitch S., Paques M., Ronco P.;
"Novel COL4A1 mutations associated with HANAC syndrome: a role for the
triple helical CB3[IV] domain.";
Am. J. Med. Genet. A 152:2550-2555(2010).
[37]
VARIANTS BSVD ASP-720 AND ARG-755.
PubMed=20385946; DOI=10.1001/archophthalmol.2010.42;
Coupry I., Sibon I., Mortemousque B., Rouanet F., Mine M., Goizet C.;
"Ophthalmological features associated with COL4A1 mutations.";
Arch. Ophthalmol. 128:483-489(2010).
[38]
VARIANT BSVD ARG-755.
PubMed=19477666; DOI=10.1016/j.ejpn.2009.04.010;
Shah S., Kumar Y., McLean B., Churchill A., Stoodley N., Rankin J.,
Rizzu P., van der Knaap M., Jardine P.;
"A dominantly inherited mutation in collagen IV A1 (COL4A1) causing
childhood onset stroke without porencephaly.";
Eur. J. Paediatr. Neurol. 14:182-187(2010).
[39]
VARIANTS LEU-7; PRO-555 AND HIS-1334.
PubMed=21527998;
Karolak J.A., Kulinska K., Nowak D.M., Pitarque J.A., Molinari A.,
Rydzanicz M., Bejjani B.A., Gajecka M.;
"Sequence variants in COL4A1 and COL4A2 genes in Ecuadorian families
with keratoconus.";
Mol. Vis. 17:827-843(2011).
-!- 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.
-!- FUNCTION: Arresten, comprising the C-terminal NC1 domain, inhibits
angiogenesis and tumor formation. The C-terminal half is found to
possess the anti-angiogenic activity. Specifically inhibits
endothelial cell proliferation, migration and tube formation.
Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2
and p38 MAPK activation. Ligand for alpha1/beta1 integrin.
-!- 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.
-!- INTERACTION:
P08572:COL4A2; NbExp=2; IntAct=EBI-2432478, EBI-2432506;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P02462-1; Sequence=Displayed;
Name=2;
IsoId=P02462-2; Sequence=VSP_034644;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in placenta.
{ECO:0000269|PubMed:10811134, ECO:0000269|PubMed:16481288}.
-!- 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: Lysines at the third position of the tripeptide repeating
unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates.
-!- 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.
-!- PTM: Proteolytic processing produces the C-terminal NC1 peptide,
arresten.
-!- DISEASE: Brain small vessel disease with or without ocular
anomalies (BSVD) [MIM:607595]: An autosomal dominant disease
characterized by weakening of the blood vessels in the brain and
retinal arteriolar tortuosity. In affected individuals, stroke is
often the first symptom and is usually caused by bleeding in the
brain (hemorrhagic stroke) rather than a lack of blood flow in the
brain (ischemic stroke). Patients also have leukoencephalopathy
and may experience seizures and migraine headaches accompanied by
visual sensations known as auras. {ECO:0000269|PubMed:16598045,
ECO:0000269|PubMed:17379824, ECO:0000269|PubMed:17696175,
ECO:0000269|PubMed:19477666, ECO:0000269|PubMed:20385946,
ECO:0000269|PubMed:22574627, ECO:0000269|PubMed:23394911,
ECO:0000269|PubMed:24628545}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Hereditary angiopathy with nephropathy aneurysms and
muscle cramps (HANAC) [MIM:611773]: The clinical renal
manifestations include hematuria and bilateral large cysts.
Histologic analysis revealed complex basement membrane defects in
kidney and skin. The systemic angiopathy appears to affect both
small vessels and large arteries. {ECO:0000269|PubMed:18160688,
ECO:0000269|PubMed:20818663}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Porencephaly 1 (POREN1) [MIM:175780]: A neurologic
disorder characterized by a fluid-filled cysts or cavities within
the cerebral hemispheres, neurologic manifestations, facial
paresis, and visual defects. Affected individuals typically have
hemiplegia, seizures, and intellectual disability. Porencephaly
type 1 is usually unilateral and results from focal destructive
lesions such as fetal vascular occlusion or birth trauma.
{ECO:0000269|PubMed:15905400, ECO:0000269|PubMed:16107487,
ECO:0000269|PubMed:19194877}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Intracerebral hemorrhage (ICH) [MIM:614519]: A
pathological condition characterized by bleeding into one or both
cerebral hemispheres including the basal ganglia and the cerebral
cortex. It is often associated with hypertension and
craniocerebral trauma. Intracerebral bleeding is a common cause of
stroke. {ECO:0000269|PubMed:22522439}. Note=Disease susceptibility
is associated with variations affecting the gene represented in
this entry.
-!- DISEASE: Tortuosity of retinal arteries (RATOR) [MIM:180000]: A
disease characterized by marked tortuosity of second- and third-
order retinal arteries with normal first-order arteries and venous
system. Most patients manifest variable degrees of symptomatic
transient vision loss due to retinal hemorrhage following minor
stress or trauma. {ECO:0000269|PubMed:25228067}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Schizencephaly (SCHZC) [MIM:269160]: Extremely rare human
congenital disorder characterized by a full-thickness cleft within
the cerebral hemispheres. These clefts are lined with gray matter
and most commonly involve the parasylvian regions. Large portions
of the cerebral hemispheres may be absent and replaced by cerebro-
spinal fluid. {ECO:0000269|PubMed:23225343}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the type IV collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00736}.
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EMBL; M26576; AAA53098.1; -; Genomic_DNA.
EMBL; J04217; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26550; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26540; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26542; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26543; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26544; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26545; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26546; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26547; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26537; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26538; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26548; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26549; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26551; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26552; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26553; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26554; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26555; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26556; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26557; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26539; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26558; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26559; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26560; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26561; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26562; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26536; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26563; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26541; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26564; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26565; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26566; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26567; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26568; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26569; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26570; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26571; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26572; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26573; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26574; AAA53098.1; JOINED; Genomic_DNA.
EMBL; M26575; AAA53098.1; JOINED; Genomic_DNA.
EMBL; AL161773; CAH71365.1; -; Genomic_DNA.
EMBL; AL390755; CAH71365.1; JOINED; Genomic_DNA.
EMBL; AL390755; CAH74130.1; -; Genomic_DNA.
EMBL; AL161773; CAH74130.1; JOINED; Genomic_DNA.
EMBL; AL161773; CAM14222.1; -; Genomic_DNA.
EMBL; AL390755; CAM14222.1; JOINED; Genomic_DNA.
EMBL; AL390755; CAM20295.1; -; Genomic_DNA.
EMBL; AL161773; CAM20295.1; JOINED; Genomic_DNA.
EMBL; BC047305; AAH47305.1; -; mRNA.
EMBL; BC151220; AAI51221.1; -; mRNA.
EMBL; X05561; CAA29075.1; -; mRNA.
EMBL; Y00706; CAA68698.1; -; mRNA.
EMBL; M10940; AAA52006.1; -; mRNA.
EMBL; M11315; AAA52042.1; -; mRNA.
EMBL; AF258349; AAF72630.1; -; mRNA.
EMBL; AF363672; AAK53382.1; -; mRNA.
EMBL; AF400431; AAK92480.1; -; mRNA.
EMBL; AY285780; AAP43112.1; -; mRNA.
EMBL; AF536207; AAM97359.1; -; mRNA.
EMBL; DQ464183; ABE73157.1; -; mRNA.
CCDS; CCDS9511.1; -. [P02462-1]
PIR; S16876; CGHU4B.
RefSeq; NP_001290039.1; NM_001303110.1.
RefSeq; NP_001836.3; NM_001845.5.
UniGene; Hs.17441; -.
PDB; 1LI1; X-ray; 1.90 A; A/B/D/E=1441-1669.
PDBsum; 1LI1; -.
ProteinModelPortal; P02462; -.
SMR; P02462; -.
BioGrid; 107679; 24.
IntAct; P02462; 26.
MINT; MINT-6743187; -.
STRING; 9606.ENSP00000364979; -.
ChEMBL; CHEMBL2364188; -.
iPTMnet; P02462; -.
PhosphoSitePlus; P02462; -.
SwissPalm; P02462; -.
BioMuta; COL4A1; -.
DMDM; 125987809; -.
EPD; P02462; -.
MaxQB; P02462; -.
PaxDb; P02462; -.
PeptideAtlas; P02462; -.
PRIDE; P02462; -.
Ensembl; ENST00000375820; ENSP00000364979; ENSG00000187498.
GeneID; 1282; -.
KEGG; hsa:1282; -.
UCSC; uc001vqw.4; human. [P02462-1]
CTD; 1282; -.
DisGeNET; 1282; -.
EuPathDB; HostDB:ENSG00000187498.14; -.
GeneCards; COL4A1; -.
GeneReviews; COL4A1; -.
HGNC; HGNC:2202; COL4A1.
HPA; CAB001695; -.
HPA; HPA054039; -.
MalaCards; COL4A1; -.
MIM; 120130; gene.
MIM; 175780; phenotype.
MIM; 180000; phenotype.
MIM; 269160; phenotype.
MIM; 607595; phenotype.
MIM; 611773; phenotype.
MIM; 614519; phenotype.
neXtProt; NX_P02462; -.
Orphanet; 73229; Autosomal dominant familial hematuria - retinal arteriolar tortuosity - contractures.
Orphanet; 99810; Familial porencephaly.
Orphanet; 36383; Familial vascular leukoencephalopathy.
Orphanet; 799; Schizencephaly.
Orphanet; 899; Walker-Warburg syndrome.
PharmGKB; PA26717; -.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410XNMM; LUCA.
HOVERGEN; HBG004933; -.
InParanoid; P02462; -.
KO; K06237; -.
OrthoDB; EOG091G0613; -.
PhylomeDB; P02462; -.
TreeFam; TF316865; -.
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-3000480; Scavenging by Class A Receptors.
Reactome; R-HSA-419037; NCAM1 interactions.
Reactome; R-HSA-8948216; Collagen chain trimerization.
SIGNOR; P02462; -.
ChiTaRS; COL4A1; human.
EvolutionaryTrace; P02462; -.
GeneWiki; Collagen,_type_IV,_alpha_1; -.
GenomeRNAi; 1282; -.
PRO; PR:P02462; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000187498; -.
CleanEx; HS_COL4A1; -.
ExpressionAtlas; P02462; baseline and differential.
Genevisible; P02462; HS.
GO; GO:0005604; C:basement membrane; IC:BHF-UCL.
GO; GO:0005587; C:collagen type IV trimer; IMP:BHF-UCL.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0030023; F:extracellular matrix constituent conferring elasticity; IC:BHF-UCL.
GO; GO:0005201; F:extracellular matrix structural constituent; IMP:BHF-UCL.
GO; GO:0048407; F:platelet-derived growth factor binding; IDA:MGI.
GO; GO:0071711; P:basement membrane organization; IMP:BHF-UCL.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:BHF-UCL.
GO; GO:0007420; P:brain development; IMP:BHF-UCL.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:BHF-UCL.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:Ensembl.
GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
GO; GO:0061333; P:renal tubule morphogenesis; IMP:BHF-UCL.
GO; GO:0061304; P:retinal blood vessel morphogenesis; IMP:BHF-UCL.
Gene3D; 2.170.240.10; -; 1.
InterPro; IPR008160; Collagen.
InterPro; IPR001442; Collagen_VI_NC.
InterPro; IPR016187; CTDL_fold.
Pfam; PF01413; C4; 2.
Pfam; PF01391; Collagen; 15.
SMART; SM00111; C4; 2.
SUPFAM; SSF56436; SSF56436; 2.
PROSITE; PS51403; NC1_IV; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Angiogenesis; Basement membrane;
Collagen; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Extracellular matrix; Glycoprotein;
Hydroxylation; Polymorphism; Reference proteome; Repeat; Secreted;
Signal.
SIGNAL 1 27 {ECO:0000269|PubMed:4043082}.
PROPEP 28 172 N-terminal propeptide (7S domain).
/FTId=PRO_0000005748.
CHAIN 173 1669 Collagen alpha-1(IV) chain.
/FTId=PRO_0000005749.
CHAIN 1445 1669 Arresten.
/FTId=PRO_0000390482.
DOMAIN 1445 1669 Collagen IV NC1. {ECO:0000255|PROSITE-
ProRule:PRU00736}.
REGION 173 1440 Triple-helical region.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
DISULFID 1460 1551 {ECO:0000255|PROSITE-ProRule:PRU00736,
ECO:0000269|PubMed:2844531}.
DISULFID 1493 1548 {ECO:0000255|PROSITE-ProRule:PRU00736,
ECO:0000269|PubMed:2844531}.
DISULFID 1505 1511 {ECO:0000255|PROSITE-ProRule:PRU00736,
ECO:0000269|PubMed:2844531}.
DISULFID 1570 1665 {ECO:0000255|PROSITE-ProRule:PRU00736,
ECO:0000269|PubMed:2844531}.
DISULFID 1604 1662 {ECO:0000255|PROSITE-ProRule:PRU00736,
ECO:0000269|PubMed:2844531}.
DISULFID 1616 1622 {ECO:0000255|PROSITE-ProRule:PRU00736,
ECO:0000269|PubMed:2844531}.
CROSSLNK 1533 1533 S-Lysyl-methionine sulfilimine (Met-Lys)
(interchain with K-1651).
CROSSLNK 1651 1651 S-Lysyl-methionine sulfilimine (Lys-Met)
(interchain with M-1533).
VAR_SEQ 498 848 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_034644.
VARIANT 7 7 V -> L (in dbSNP:rs9515185).
{ECO:0000269|PubMed:21527998}.
/FTId=VAR_030027.
VARIANT 144 144 A -> V. {ECO:0000269|PubMed:22522439}.
/FTId=VAR_073809.
VARIANT 304 304 P -> L (in dbSNP:rs34843786).
/FTId=VAR_044158.
VARIANT 352 352 P -> L (in ICH; the mutant protein is
retained intracellularly and is not
secreted normally).
{ECO:0000269|PubMed:22522439}.
/FTId=VAR_073810.
VARIANT 498 498 G -> R (in HANAC).
{ECO:0000269|PubMed:20818663}.
/FTId=VAR_064493.
VARIANT 498 498 G -> V (in HANAC).
{ECO:0000269|PubMed:18160688}.
/FTId=VAR_044159.
VARIANT 510 510 G -> R (in HANAC and RATOR).
{ECO:0000269|PubMed:20818663,
ECO:0000269|PubMed:25228067}.
/FTId=VAR_064494.
VARIANT 519 519 G -> R (in HANAC).
{ECO:0000269|PubMed:18160688}.
/FTId=VAR_044160.
VARIANT 525 525 G -> L (in HANAC; requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:20818663}.
/FTId=VAR_064495.
VARIANT 528 528 G -> E (in HANAC).
{ECO:0000269|PubMed:18160688}.
/FTId=VAR_044161.
VARIANT 538 538 R -> G (in ICH; the mutant protein is
retained intracellularly and is not
secreted normally).
{ECO:0000269|PubMed:22522439}.
/FTId=VAR_073811.
VARIANT 555 555 T -> P (in dbSNP:rs536174).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:21527998,
ECO:0000269|PubMed:2701944,
ECO:0000269|PubMed:3311751,
ECO:0000269|PubMed:3691802}.
/FTId=VAR_030511.
VARIANT 562 562 G -> E (in BSVD).
{ECO:0000269|PubMed:16598045}.
/FTId=VAR_030028.
VARIANT 655 655 G -> R (in SCHZC).
{ECO:0000269|PubMed:23225343}.
/FTId=VAR_073812.
VARIANT 708 708 G -> R (in BSVD).
{ECO:0000269|PubMed:24628545}.
/FTId=VAR_073813.
VARIANT 720 720 G -> D (in BSVD; diffuse small vessel
disease of the brain associated with
Axenfeld-Rieger anomaly and
leukoencephalopathy).
{ECO:0000269|PubMed:17696175,
ECO:0000269|PubMed:20385946}.
/FTId=VAR_064496.
VARIANT 749 749 G -> S (in POREN1).
{ECO:0000269|PubMed:15905400}.
/FTId=VAR_030029.
VARIANT 755 755 G -> R (in BSVD; associated with ocular
anomalies of variable severity in some
patients). {ECO:0000269|PubMed:19477666,
ECO:0000269|PubMed:20385946,
ECO:0000269|PubMed:22574627}.
/FTId=VAR_064497.
VARIANT 773 773 G -> R (in BSVD).
{ECO:0000269|PubMed:22574627,
ECO:0000269|PubMed:24628545}.
/FTId=VAR_073814.
VARIANT 805 805 G -> R (in BSVD).
{ECO:0000269|PubMed:17379824}.
/FTId=VAR_064498.
VARIANT 870 870 G -> R (in SCHZC).
{ECO:0000269|PubMed:23225343}.
/FTId=VAR_073815.
VARIANT 882 882 G -> D (in BSVD).
{ECO:0000269|PubMed:22574627}.
/FTId=VAR_073816.
VARIANT 897 897 G -> S (in SCHZC).
{ECO:0000269|PubMed:23225343}.
/FTId=VAR_073817.
VARIANT 948 948 G -> S (in SCHZC).
{ECO:0000269|PubMed:23225343}.
/FTId=VAR_073818.
VARIANT 1041 1041 G -> E (in SCHZC).
{ECO:0000269|PubMed:23225343}.
/FTId=VAR_073819.
VARIANT 1082 1082 G -> E (in SCHZC).
{ECO:0000269|PubMed:23225343}.
/FTId=VAR_073820.
VARIANT 1130 1130 G -> D (in POREN1).
{ECO:0000269|PubMed:16107487}.
/FTId=VAR_030030.
VARIANT 1236 1236 G -> R (in POREN1).
{ECO:0000269|PubMed:15905400}.
/FTId=VAR_030031.
VARIANT 1266 1266 G -> R (in BSVD).
{ECO:0000269|PubMed:22574627}.
/FTId=VAR_073821.
VARIANT 1326 1326 G -> R (in SCHZC).
{ECO:0000269|PubMed:23225343}.
/FTId=VAR_073822.
VARIANT 1332 1332 G -> D (in SCHZC).
{ECO:0000269|PubMed:23225343}.
/FTId=VAR_073823.
VARIANT 1334 1334 Q -> H (in dbSNP:rs3742207).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:21527998}.
/FTId=VAR_020013.
VARIANT 1423 1423 G -> R (in POREN1).
{ECO:0000269|PubMed:16107487}.
/FTId=VAR_030032.
VARIANT 1531 1531 M -> V. {ECO:0000269|PubMed:22522439}.
/FTId=VAR_073824.
VARIANT 1580 1580 G -> R (in POREN1).
{ECO:0000269|PubMed:19194877}.
/FTId=VAR_064499.
VARIANT 1615 1615 E -> K (in SCHZC).
{ECO:0000269|PubMed:23225343}.
/FTId=VAR_073825.
VARIANT 1627 1627 N -> K (in BSVD).
{ECO:0000269|PubMed:23394911}.
/FTId=VAR_073826.
CONFLICT 237 238 SG -> KE (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 241 241 G -> K (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 319 319 Q -> A (in Ref. 4; CAA29075).
{ECO:0000305}.
CONFLICT 719 719 N -> D (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 837 837 D -> Y (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 842 842 K -> P (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 896 896 V -> W (in Ref. 7; CAA68698).
{ECO:0000305}.
CONFLICT 904 904 E -> Q (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 914 914 S -> K (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 998 998 S -> K (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 1010 1010 K -> P (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 1012 1012 S -> K (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 1358 1358 E -> Q (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 1490 1490 A -> T (in Ref. 17; ABE73157).
{ECO:0000305}.
CONFLICT 1507 1507 I -> T (in Ref. 17; ABE73157).
{ECO:0000305}.
CONFLICT 1519 1519 Y -> C (in Ref. 17; ABE73157).
{ECO:0000305}.
CONFLICT 1570 1570 C -> Y (in Ref. 16; AAM97359).
{ECO:0000305}.
STRAND 1446 1451 {ECO:0000244|PDB:1LI1}.
STRAND 1453 1456 {ECO:0000244|PDB:1LI1}.
STRAND 1465 1478 {ECO:0000244|PDB:1LI1}.
STRAND 1481 1484 {ECO:0000244|PDB:1LI1}.
HELIX 1490 1492 {ECO:0000244|PDB:1LI1}.
STRAND 1493 1496 {ECO:0000244|PDB:1LI1}.
STRAND 1502 1505 {ECO:0000244|PDB:1LI1}.
STRAND 1509 1514 {ECO:0000244|PDB:1LI1}.
STRAND 1519 1524 {ECO:0000244|PDB:1LI1}.
HELIX 1538 1544 {ECO:0000244|PDB:1LI1}.
STRAND 1547 1555 {ECO:0000244|PDB:1LI1}.
STRAND 1557 1561 {ECO:0000244|PDB:1LI1}.
STRAND 1563 1566 {ECO:0000244|PDB:1LI1}.
STRAND 1574 1587 {ECO:0000244|PDB:1LI1}.
HELIX 1589 1591 {ECO:0000244|PDB:1LI1}.
STRAND 1593 1595 {ECO:0000244|PDB:1LI1}.
HELIX 1601 1603 {ECO:0000244|PDB:1LI1}.
STRAND 1604 1607 {ECO:0000244|PDB:1LI1}.
STRAND 1613 1617 {ECO:0000244|PDB:1LI1}.
STRAND 1620 1623 {ECO:0000244|PDB:1LI1}.
STRAND 1629 1634 {ECO:0000244|PDB:1LI1}.
HELIX 1638 1640 {ECO:0000244|PDB:1LI1}.
STRAND 1648 1651 {ECO:0000244|PDB:1LI1}.
HELIX 1655 1658 {ECO:0000244|PDB:1LI1}.
STRAND 1661 1667 {ECO:0000244|PDB:1LI1}.
SEQUENCE 1669 AA; 160615 MW; 3C9BCD8E410A9ED1 CRC64;
MGPRLSVWLL LLPAALLLHE EHSRAAAKGG CAGSGCGKCD CHGVKGQKGE RGLPGLQGVI
GFPGMQGPEG PQGPPGQKGD TGEPGLPGTK GTRGPPGASG YPGNPGLPGI PGQDGPPGPP
GIPGCNGTKG ERGPLGPPGL PGFAGNPGPP GLPGMKGDPG EILGHVPGML LKGERGFPGI
PGTPGPPGLP GLQGPVGPPG FTGPPGPPGP PGPPGEKGQM GLSFQGPKGD KGDQGVSGPP
GVPGQAQVQE KGDFATKGEK GQKGEPGFQG MPGVGEKGEP GKPGPRGKPG KDGDKGEKGS
PGFPGEPGYP GLIGRQGPQG EKGEAGPPGP PGIVIGTGPL GEKGERGYPG TPGPRGEPGP
KGFPGLPGQP GPPGLPVPGQ AGAPGFPGER GEKGDRGFPG TSLPGPSGRD GLPGPPGSPG
PPGQPGYTNG IVECQPGPPG DQGPPGIPGQ PGFIGEIGEK GQKGESCLIC DIDGYRGPPG
PQGPPGEIGF PGQPGAKGDR GLPGRDGVAG VPGPQGTPGL IGQPGAKGEP GEFYFDLRLK
GDKGDPGFPG QPGMTGRAGS PGRDGHPGLP GPKGSPGSVG LKGERGPPGG VGFPGSRGDT
GPPGPPGYGP AGPIGDKGQA GFPGGPGSPG LPGPKGEPGK IVPLPGPPGA EGLPGSPGFP
GPQGDRGFPG TPGRPGLPGE KGAVGQPGIG FPGPPGPKGV DGLPGDMGPP GTPGRPGFNG
LPGNPGVQGQ KGEPGVGLPG LKGLPGLPGI PGTPGEKGSI GVPGVPGEHG AIGPPGLQGI
RGEPGPPGLP GSVGSPGVPG IGPPGARGPP GGQGPPGLSG PPGIKGEKGF PGFPGLDMPG
PKGDKGAQGL PGITGQSGLP GLPGQQGAPG IPGFPGSKGE MGVMGTPGQP GSPGPVGAPG
LPGEKGDHGF PGSSGPRGDP GLKGDKGDVG LPGKPGSMDK VDMGSMKGQK GDQGEKGQIG
PIGEKGSRGD PGTPGVPGKD GQAGQPGQPG PKGDPGISGT PGAPGLPGPK GSVGGMGLPG
TPGEKGVPGI PGPQGSPGLP GDKGAKGEKG QAGPPGIGIP GLRGEKGDQG IAGFPGSPGE
KGEKGSIGIP GMPGSPGLKG SPGSVGYPGS PGLPGEKGDK GLPGLDGIPG VKGEAGLPGT
PGPTGPAGQK GEPGSDGIPG SAGEKGEPGL PGRGFPGFPG AKGDKGSKGE VGFPGLAGSP
GIPGSKGEQG FMGPPGPQGQ PGLPGSPGHA TEGPKGDRGP QGQPGLPGLP GPMGPPGLPG
IDGVKGDKGN PGWPGAPGVP GPKGDPGFQG MPGIGGSPGI TGSKGDMGPP GVPGFQGPKG
LPGLQGIKGD QGDQGVPGAK GLPGPPGPPG PYDIIKGEPG LPGPEGPPGL KGLQGLPGPK
GQQGVTGLVG IPGPPGIPGF DGAPGQKGEM GPAGPTGPRG FPGPPGPDGL PGSMGPPGTP
SVDHGFLVTR HSQTIDDPQC PSGTKILYHG YSLLYVQGNE RAHGQDLGTA GSCLRKFSTM
PFLFCNINNV CNFASRNDYS YWLSTPEPMP MSMAPITGEN IRPFISRCAV CEAPAMVMAV
HSQTIQIPPC PSGWSSLWIG YSFVMHTSAG AEGSGQALAS PGSCLEEFRS APFIECHGRG
TCNYYANAYS FWLATIERSE MFKKPTPSTL KAGELRTHVS RCQVCMRRT


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Catalog number Product name Quantity
L0227-2 Collagen type IV alpha 3 chain (cleaved) Rabbit antibody Ab Aff - Purified 0.1 mg
L0228-2 Collagen type IV alpha 3 chain (cleaved) Rabbit antibody Ab Aff - Purified 0.1 mg
'L0220-2 Collagen type I alpha 2 chain (cleaved) antibody Ab host: Rabbit 0.1 mg
L0211-1 Collagen type III alpha 1 chain (cleaved) Rabbit antibody Ab Aff - Purified 50
L0211-2 Collagen type III alpha 1 chain (cleaved) Rabbit antibody Ab Aff - Purified 0.1 mg
L0220-1 Collagen type I alpha 2 chain (cleaved) Rabbit antibody Ab Aff - Purified 50
L0220-2 Collagen type I alpha 2 chain (cleaved) Rabbit antibody Ab Aff - Purified 0.1 mg
L0227-1 Collagen type IV alpha 3 chain (cleaved) Rabbit antibody Ab Aff - Purified 50
L0228-1 Collagen type IV alpha 3 chain (cleaved) Rabbit antibody Ab Aff - Purified 50
'L0228-1 Collagen type IV alpha 3 chain (cleaved) antibody Ab host: Rabbit 50 Вµg
'L0227-1 Collagen type IV alpha 3 chain (cleaved) antibody Ab host: Rabbit 50 Вµg
'L0211-1 Collagen type III alpha 1 chain (cleaved) antibody Ab host: Rabbit 50 Вµg
'L0228-2 Collagen type IV alpha 3 chain (cleaved) antibody Ab host: Rabbit 0.1 mg
'L0211-2 Collagen type III alpha 1 chain (cleaved) antibody Ab host: Rabbit 0.1 mg
'L0227-2 Collagen type IV alpha 3 chain (cleaved) antibody Ab host: Rabbit 0.1 mg
'L0220-1 Collagen type I alpha 2 chain (cleaved) antibody Ab host: Rabbit 50 Вµg
EIAAB08410 COL29A1,COL6A5,Collagen alpha-1(XXIX) chain,Collagen alpha-5(VI) chain,Homo sapiens,Human,von Willebrand factor A domain-containing protein 4,VWA4
EIAAB08414 COL7A1,Collagen alpha-1(VII) chain,Homo sapiens,Human,LC collagen,Long-chain collagen
EIAAB08411 Col29a1,Col6a5,Collagen alpha-1(XXIX) chain,Collagen alpha-5(VI) chain,Gm7455,Mouse,Mus musculus
EIAAB08415 Col7a1,Collagen alpha-1(VII) chain,LC collagen,Long-chain collagen,Mouse,Mus musculus
EIAAB08519 COL19A1,Collagen alpha-1(XIX) chain,Collagen alpha-1(Y) chain,Homo sapiens,Human
EIAAB08518 Col19a1,Collagen alpha-1(XIX) chain,Collagen alpha-1(Y) chain,Mouse,Mus musculus
E0571h ELISA kit Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Homo sapiens,Human 96T
E0571m ELISA kit Alpha-1 type I collagen,Col1a1,Cola1,Collagen alpha-1(I) chain,Mouse,Mus musculus 96T
E0571Rb ELISA kit Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Oryctolagus cuniculus,Rabbit 96T


 

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