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Collagen alpha-1(XII) chain

 COCA1_HUMAN             Reviewed;        3063 AA.
Q99715; O43853; Q15955; Q5VYK1; Q5VYK2; Q71UR3; Q99716;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 2.
02-JUN-2021, entry version 200.
RecName: Full=Collagen alpha-1(XII) chain;
Flags: Precursor;
Name=COL12A1; Synonyms=COL12A1L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF
1280-1295; 1782-1801 AND 2906-2916, AND VARIANT SER-3058.
PubMed=9143499; DOI=10.1006/geno.1997.4638;
Gerecke D.R., Olson P.F., Koch M., Knoll J.H.M., Taylor R., Hudson D.L.,
Champliaud M.-F., Olsen B.R., Burgeson R.E.;
"Complete primary structure of two splice variants of collagen XII, and
assignment of alpha 1(XII) collagen (COL12A1), alpha 1(IX) collagen
(COL9A1), and alpha 1(XIX) collagen (COL19A1) to human chromosome 6q12-
q13.";
Genomics 41:236-242(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
PubMed=9826181; DOI=10.1046/j.1432-1327.1998.2570362.x;
Chiquet M., Mumenthaler U., Wittwer M., Jin W., Koch M.;
"The chick and human collagen alpha1(XII) gene promoter -- activity of
highly conserved regions around the first exon and in the first intron.";
Eur. J. Biochem. 257:362-371(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 299-816 (ISOFORMS 1/4), AND TISSUE
SPECIFICITY.
TISSUE=Cornea;
PubMed=9344363;
Wessel H., Anderson S., Fite D., Halvas E., Hempel J., SundarRaj N.;
"Type XII collagen contributes to diversities in human corneal and limbal
extracellular matrices.";
Invest. Ophthalmol. Vis. Sci. 38:2408-2422(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2567-2755 (ISOFORM 4).
PubMed=1427837; DOI=10.1016/s0888-7543(05)80210-1;
Oh S.P., Taylor R.W., Gerecke D.R., Rochelle J.M., Seldin M.F., Olsen B.R.;
"The mouse alpha 1(XII) and human alpha 1(XII)-like collagen genes are
localized on mouse chromosome 9 and human chromosome 6.";
Genomics 14:225-231(1992).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2528 AND ASN-2679.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple
enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
INVOLVEMENT IN UCMD2, INVOLVEMENT IN BTHLM2, AND VARIANT BTHLM2 THR-2334.
PubMed=24334604; DOI=10.1093/hmg/ddt627;
Zou Y., Zwolanek D., Izu Y., Gandhy S., Schreiber G., Brockmann K.,
Devoto M., Tian Z., Hu Y., Veit G., Meier M., Stetefeld J., Hicks D.,
Straub V., Voermans N.C., Birk D.E., Barton E.R., Koch M., Boennemann C.G.;
"Recessive and dominant mutations in COL12A1 cause a novel EDS/myopathy
overlap syndrome in humans and mice.";
Hum. Mol. Genet. 23:2339-2352(2014).
[9]
INVOLVEMENT IN BTHLM2, VARIANTS BTHLM2 CYS-1965 AND ASP-2786, AND VARIANTS
THR-1738 AND SER-3058.
PubMed=24334769; DOI=10.1093/hmg/ddt637;
Hicks D., Farsani G.T., Laval S., Collins J., Sarkozy A., Martoni E.,
Shah A., Zou Y., Koch M., Boennemann C.G., Roberts M., Lochmueller H.,
Bushby K., Straub V.;
"Mutations in the collagen XII gene define a new form of extracellular
matrix-related myopathy.";
Hum. Mol. Genet. 23:2353-2363(2014).
[10]
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).
-!- FUNCTION: Type XII collagen interacts with type I collagen-containing
fibrils, the COL1 domain could be associated with the surface of the
fibrils, and the COL2 and NC3 domains may be localized in the
perifibrillar matrix. {ECO:0000250}.
-!- SUBUNIT: Trimer of identical chains each containing 190 kDa of non-
triple-helical sequences.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=The final tissue form of collagen XII may contain homotrimers
of either isoform 1 or isoform 2 or any combination of isoform 1 and
isoform 2.;
Name=1; Synonyms=Long;
IsoId=Q99715-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=Q99715-2; Sequence=VSP_001149;
Name=4;
IsoId=Q99715-4; Sequence=VSP_024942;
-!- TISSUE SPECIFICITY: Found in collagen I-containing tissues: both
isoform 1 and isoform 2 appear in amnion, chorion, skeletal muscle,
small intestine, and in cell culture of dermal fibroblasts,
keratinocytes and endothelial cells. Only isoform 2 is found in lung,
placenta, kidney and a squamous cell carcinoma cell line. Isoform 1 is
also present in the corneal epithelial Bowman's membrane (BM) and the
interfibrillar matrix of the corneal stroma, but it is not detected in
the limbal BM. {ECO:0000269|PubMed:9344363}.
-!- PTM: The triple-helical tail is stabilized by disulfide bonds at each
end. {ECO:0000250}.
-!- PTM: Hydroxylation on proline residues within the sequence motif, GXPG,
is most likely to be 4-hydroxy as this fits the requirement for 4-
hydroxylation in vertebrates. {ECO:0000250}.
-!- PTM: Isoform 1 O-glycosylation; glycosaminoglycan of chondroitin-
sulfate type. {ECO:0000250}.
-!- DISEASE: Ullrich congenital muscular dystrophy 2 (UCMD2) [MIM:616470]:
A form of Ullrich muscular dystrophy, a congenital myopathy
characterized by muscle weakness and multiple joint contractures,
generally noted at birth or early infancy. The clinical course is more
severe than in Bethlem myopathy. {ECO:0000269|PubMed:24334604}.
Note=The disease is caused by variants affecting the gene represented
in this entry.
-!- DISEASE: Bethlem myopathy 2 (BTHLM2) [MIM:616471]: A form of Bethlem
myopathy, a benign proximal myopathy characterized by early childhood
onset and joint contractures most frequently affecting the elbows and
ankles. BTHLM2 inheritance is autosomal dominant.
{ECO:0000269|PubMed:24334604, ECO:0000269|PubMed:24334769}. Note=The
disease is caused by variants affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
helices (FACIT) family. {ECO:0000305}.
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EMBL; U73778; AAC51244.1; -; mRNA.
EMBL; U73779; AAD40483.1; -; mRNA.
EMBL; AL080250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL354664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL096771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF061871; AAC83578.1; -; Genomic_DNA.
EMBL; U68139; AAC01506.1; -; mRNA.
EMBL; AH004088; AAB23937.2; -; Genomic_DNA.
CCDS; CCDS43481.1; -. [Q99715-2]
CCDS; CCDS43482.1; -. [Q99715-1]
PIR; A44479; A44479.
RefSeq; NP_004361.3; NM_004370.5. [Q99715-1]
RefSeq; NP_542376.2; NM_080645.2. [Q99715-2]
SMR; Q99715; -.
BioGRID; 107700; 11.
ComplexPortal; CPX-1753; Collagen type XII trimer.
IntAct; Q99715; 9.
STRING; 9606.ENSP00000325146; -.
GlyConnect; 1131; 70 N-Linked glycans (4 sites).
GlyGen; Q99715; 13 sites, 17 N-linked glycans (2 sites), 8 O-linked glycans (5 sites).
iPTMnet; Q99715; -.
PhosphoSitePlus; Q99715; -.
BioMuta; COL12A1; -.
DMDM; 146345397; -.
EPD; Q99715; -.
jPOST; Q99715; -.
MassIVE; Q99715; -.
MaxQB; Q99715; -.
PaxDb; Q99715; -.
PeptideAtlas; Q99715; -.
PRIDE; Q99715; -.
ProteomicsDB; 78429; -. [Q99715-1]
ProteomicsDB; 78430; -. [Q99715-2]
ProteomicsDB; 78431; -. [Q99715-4]
Antibodypedia; 2124; 91 antibodies.
DNASU; 1303; -.
Ensembl; ENST00000322507; ENSP00000325146; ENSG00000111799. [Q99715-1]
Ensembl; ENST00000345356; ENSP00000305147; ENSG00000111799. [Q99715-2]
Ensembl; ENST00000416123; ENSP00000412864; ENSG00000111799. [Q99715-4]
GeneID; 1303; -.
KEGG; hsa:1303; -.
UCSC; uc063ppm.1; human. [Q99715-1]
CTD; 1303; -.
DisGeNET; 1303; -.
GeneCards; COL12A1; -.
HGNC; HGNC:2188; COL12A1.
HPA; ENSG00000111799; Tissue enhanced (breast).
MalaCards; COL12A1; -.
MIM; 120320; gene.
MIM; 616470; phenotype.
MIM; 616471; phenotype.
neXtProt; NX_Q99715; -.
OpenTargets; ENSG00000111799; -.
Orphanet; 610; Bethlem myopathy.
Orphanet; 75840; Congenital muscular dystrophy, Ullrich type.
Orphanet; 536516; Myopathic Ehlers-Danlos syndrome.
PharmGKB; PA26704; -.
VEuPathDB; HostDB:ENSG00000111799.20; -.
eggNOG; KOG3544; Eukaryota.
GeneTree; ENSGT00940000154923; -.
HOGENOM; CLU_000467_0_0_1; -.
InParanoid; Q99715; -.
OMA; VKVSTEC; -.
OrthoDB; 67372at2759; -.
PhylomeDB; Q99715; -.
TreeFam; TF329914; -.
PathwayCommons; Q99715; -.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-8948216; Collagen chain trimerization.
SIGNOR; Q99715; -.
BioGRID-ORCS; 1303; 3 hits in 988 CRISPR screens.
ChiTaRS; COL12A1; human.
GeneWiki; Collagen,_type_XII,_alpha_1; -.
GenomeRNAi; 1303; -.
Pharos; Q99715; Tbio.
PRO; PR:Q99715; -.
Proteomes; UP000005640; Chromosome 6.
RNAct; Q99715; protein.
Bgee; ENSG00000111799; Expressed in tibia and 206 other tissues.
ExpressionAtlas; Q99715; baseline and differential.
Genevisible; Q99715; HS.
GO; GO:0005595; C:collagen type XII trimer; TAS:ProtInc.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; NAS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0030199; P:collagen fibril organization; TAS:Reactome.
GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
CDD; cd00063; FN3; 18.
Gene3D; 2.60.40.10; -; 18.
Gene3D; 3.40.50.410; -; 4.
InterPro; IPR008160; Collagen.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR001791; Laminin_G.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF01391; Collagen; 4.
Pfam; PF00041; fn3; 18.
Pfam; PF00092; VWA; 4.
SMART; SM00060; FN3; 18.
SMART; SM00210; TSPN; 1.
SMART; SM00327; VWA; 4.
SUPFAM; SSF49265; SSF49265; 11.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF53300; SSF53300; 4.
PROSITE; PS50853; FN3; 18.
PROSITE; PS50234; VWFA; 4.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Collagen;
Congenital muscular dystrophy; Direct protein sequencing; Disease variant;
Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation;
Proteoglycan; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1..23
/evidence="ECO:0000255"
CHAIN 24..3063
/note="Collagen alpha-1(XII) chain"
/id="PRO_0000005783"
DOMAIN 27..117
/note="Fibronectin type-III 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 140..316
/note="VWFA 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
DOMAIN 336..426
/note="Fibronectin type-III 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 440..616
/note="VWFA 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
DOMAIN 634..722
/note="Fibronectin type-III 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 725..816
/note="Fibronectin type-III 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 817..905
/note="Fibronectin type-III 5"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 907..998
/note="Fibronectin type-III 6"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 999..1087
/note="Fibronectin type-III 7"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 1089..1179
/note="Fibronectin type-III 8"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 1199..1371
/note="VWFA 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
DOMAIN 1387..1476
/note="Fibronectin type-III 9"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 1477..1567
/note="Fibronectin type-III 10"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 1568..1658
/note="Fibronectin type-III 11"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 1659..1754
/note="Fibronectin type-III 12"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 1755..1849
/note="Fibronectin type-III 13"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 1850..1935
/note="Fibronectin type-III 14"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 1936..2026
/note="Fibronectin type-III 15"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 2027..2117
/note="Fibronectin type-III 16"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 2118..2206
/note="Fibronectin type-III 17"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 2207..2294
/note="Fibronectin type-III 18"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 2323..2496
/note="VWFA 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
DOMAIN 2520..2712
/note="Laminin G-like"
DOMAIN 2747..2798
/note="Collagen-like 1"
DOMAIN 2802..2852
/note="Collagen-like 2"
DOMAIN 2853..2898
/note="Collagen-like 3"
DOMAIN 2941..2990
/note="Collagen-like 4"
REGION 799..830
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1077..1099
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 2283..2312
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 2451..2746
/note="Nonhelical region (NC3)"
REGION 2743..2896
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 2747..2898
/note="Triple-helical region (COL2) with 1 imperfection"
REGION 2899..2941
/note="Nonhelical region (NC2)"
REGION 2932..3063
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 2942..3044
/note="Triple-helical region (COL1) with 2 imperfections"
REGION 3045..3063
/note="Nonhelical region (NC1)"
MOTIF 862..864
/note="Cell attachment site"
/evidence="ECO:0000255"
MOTIF 2779..2781
/note="Cell attachment site"
/evidence="ECO:0000255"
MOTIF 2895..2897
/note="Cell attachment site"
/evidence="ECO:0000255"
COMPBIAS 1078..1099
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 2297..2312
/note="Pro residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 2778..2797
/note="Pro residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 2824..2838
/note="Pro residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 2940..2954
/note="Pro residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 3018..3036
/note="Pro residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 3048..3063
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 2944
/note="4-hydroxyproline"
/evidence="ECO:0000250"
MOD_RES 2947
/note="4-hydroxyproline"
/evidence="ECO:0000250"
MOD_RES 2950
/note="4-hydroxyproline"
/evidence="ECO:0000250"
MOD_RES 2959
/note="4-hydroxyproline"
/evidence="ECO:0000250"
MOD_RES 2965
/note="4-hydroxyproline"
/evidence="ECO:0000250"
MOD_RES 2968
/note="4-hydroxyproline"
/evidence="ECO:0000250"
MOD_RES 2971
/note="4-hydroxyproline"
/evidence="ECO:0000250"
MOD_RES 2983
/note="4-hydroxyproline"
/evidence="ECO:0000250"
MOD_RES 3000
/note="4-hydroxyproline"
/evidence="ECO:0000250"
MOD_RES 3003
/note="4-hydroxyproline"
/evidence="ECO:0000250"
MOD_RES 3014
/note="4-hydroxyproline"
/evidence="ECO:0000250"
MOD_RES 3023
/note="4-hydroxyproline"
/evidence="ECO:0000250"
MOD_RES 3026
/note="4-hydroxyproline"
/evidence="ECO:0000250"
MOD_RES 3029
/note="4-hydroxyproline"
/evidence="ECO:0000250"
CARBOHYD 700
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 798
/note="O-linked (Xyl...) (chondroitin sulfate) serine"
/evidence="ECO:0000255"
CARBOHYD 889
/note="O-linked (Xyl...) (chondroitin sulfate) serine"
/evidence="ECO:0000255"
CARBOHYD 981
/note="O-linked (Xyl...) (chondroitin sulfate) serine"
/evidence="ECO:0000255"
CARBOHYD 1763
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2206
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2528
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 2679
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
VAR_SEQ 25..1188
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:9143499"
/id="VSP_001149"
VAR_SEQ 2651..2726
/note="Missing (in isoform 4)"
/evidence="ECO:0000305"
/id="VSP_024942"
VARIANT 461
/note="A -> P (in dbSNP:rs34730529)"
/id="VAR_048768"
VARIANT 1738
/note="I -> T (in dbSNP:rs240736)"
/evidence="ECO:0000269|PubMed:24334769"
/id="VAR_048769"
VARIANT 1965
/note="R -> C (in BTHLM2; unknown pathological
significance; dbSNP:rs200487396)"
/evidence="ECO:0000269|PubMed:24334769"
/id="VAR_074546"
VARIANT 2021
/note="R -> Q (in dbSNP:rs34438461)"
/id="VAR_061111"
VARIANT 2160
/note="E -> V (in dbSNP:rs35523808)"
/id="VAR_048770"
VARIANT 2334
/note="I -> T (in BTHLM2; dbSNP:rs796052093)"
/evidence="ECO:0000269|PubMed:24334604"
/id="VAR_074547"
VARIANT 2596
/note="I -> V (in dbSNP:rs35710072)"
/id="VAR_048771"
VARIANT 2786
/note="G -> D (in BTHLM2; dbSNP:rs796052094)"
/evidence="ECO:0000269|PubMed:24334769"
/id="VAR_074548"
VARIANT 3048
/note="Q -> H (in dbSNP:rs57396313)"
/id="VAR_061112"
VARIANT 3058
/note="G -> S (in dbSNP:rs970547)"
/evidence="ECO:0000269|PubMed:24334769,
ECO:0000269|PubMed:9143499"
/id="VAR_074549"
CONFLICT 47
/note="K -> E (in Ref. 1; AAC51244)"
/evidence="ECO:0000305"
CONFLICT 441..442
/note="IV -> M (in Ref. 4; AAC01506)"
/evidence="ECO:0000305"
CONFLICT 581
/note="R -> D (in Ref. 4; AAC01506)"
/evidence="ECO:0000305"
CONFLICT 689
/note="S -> N (in Ref. 4; AAC01506)"
/evidence="ECO:0000305"
CONFLICT 743
/note="W -> S (in Ref. 4; AAC01506)"
/evidence="ECO:0000305"
CONFLICT 749
/note="R -> K (in Ref. 4; AAC01506)"
/evidence="ECO:0000305"
CONFLICT 753
/note="Y -> C (in Ref. 1; AAC51244)"
/evidence="ECO:0000305"
CONFLICT 813
/note="V -> G (in Ref. 4; AAC01506)"
/evidence="ECO:0000305"
CONFLICT 1355
/note="A -> D (in Ref. 1; AAC51244)"
/evidence="ECO:0000305"
CONFLICT 1690
/note="A -> G (in Ref. 1; AAC51244)"
/evidence="ECO:0000305"
CONFLICT 1729
/note="P -> A (in Ref. 1; AAC51244)"
/evidence="ECO:0000305"
CONFLICT 1949..1951
/note="SLD -> RLG (in Ref. 1; AAC51244)"
/evidence="ECO:0000305"
CONFLICT 2614
/note="P -> S (in Ref. 5; AAB23937)"
/evidence="ECO:0000305"
CONFLICT 2647..2648
/note="SF -> RK (in Ref. 5; AAB23937)"
/evidence="ECO:0000305"
CONFLICT 2848
/note="G -> S (in Ref. 1; AAC51244)"
/evidence="ECO:0000305"
CONFLICT 2858
/note="P -> R (in Ref. 1; AAC51244)"
/evidence="ECO:0000305"
CONFLICT 3035
/note="R -> Q (in Ref. 1; AAC51244)"
/evidence="ECO:0000305"
SEQUENCE 3063 AA; 333147 MW; EA38CAFECE8393D2 CRC64;
MRSRLPPALA ALGAALLLSS IEAEVDPPSD LNFKIIDENT VHMSWAKPVD PIVGYRITVD
PTTDGPTKEF TLSASTTETL LSELVPETEY VVTITSYDEV EESVPVIGQL TIQTGSSTKP
VEKKPGKTEI QKCSVSAWTD LVFLVDGSWS VGRNNFKYIL DFIAALVSAF DIGEEKTRVG
VVQYSSDTRT EFNLNQYYQR DELLAAIKKI PYKGGNTMTG DAIDYLVKNT FTESAGARVG
FPKVAIIITD GKSQDEVEIP ARELRNVGVE VFSLGIKAAD AKELKQIAST PSLNHVFNVA
NFDAIVDIQN EIISQVCSGV DEQLGELVSG EEVVEPPSNL IAMEVSSKYV KLNWNPSPSP
VTGYKVILTP MTAGSRQHAL SVGPQTTTLS VRDLSADTEY QISVSAMKGM TSSEPISIME
KTQPMKVQVE CSRGVDIKAD IVFLVDGSYS IGIANFVKVR AFLEVLVKSF EISPNRVQIS
LVQYSRDPHT EFTLKKFTKV EDIIEAINTF PYRGGSTNTG KAMTYVREKI FVPSKGSRSN
VPKVMILITD GKSSDAFRDP AIKLRNSDVE IFAVGVKDAV RSELEAIASP PAETHVFTVE
DFDAFQRISF ELTQSICLRI EQELAAIKKK AYVPPKDLSF SEVTSYGFKT NWSPAGENVF
SYHITYKEAA GDDEVTVVEP ASSTSVVLSS LKPETLYLVN VTAEYEDGFS IPLAGEETTE
EVKGAPRNLK VTDETTDSFK ITWTQAPGRV LRYRIIYRPV AGGESREVTT PPNQRRRTLE
NLIPDTKYEV SVIPEYFSGP GTPLTGNAAT EEVRGNPRDL RVSDPTTSTM KLSWSGAPGK
VKQYLVTYTP VAGGETQEVT VRGDTTNTVL QGLKEGTQYA LSVTALYASG AGDALFGEGT
TLEERGSPQD LVTKDITDTS IGAYWTSAPG MVRGYRVSWK SLYDDVDTGE KNLPEDAIHT
MIENLQPETK YRISVFATYS SGEGEPLTGD ATTELSQDSK TLKVDEETEN TMRVTWKPAP
GKVVNYRVVY RPHGRGKQMV AKVPPTVTST VLKRLQPQTT YDITVLPIYK MGEGKLRQGS
GTTASRFKSP RNLKTSDPTM SSFRVTWEPA PGEVKGYKVT FHPTGDDRRL GELVVGPYDN
TVVLEELRAG TTYKVNVFGM FDGGESSPLV GQEMTTLSDT TVMPILSSGM ECLTRAEADI
VLLVDGSWSI GRANFRTVRS FISRIVEVFD IGPKRVQIAL AQYSGDPRTE WQLNAHRDKK
SLLQAVANLP YKGGNTLTGM ALNFIRQQNF RTQAGMRPRA RKIGVLITDG KSQDDVEAPS
KKLKDEGVEL FAIGIKNADE VELKMIATDP DDTHAYNVAD FESLSRIVDD LTINLCNSVK
GPGDLEAPSN LVISERTHRS FRVSWTPPSD SVDRYKVEYY PVSGGKRQEF YVSRMETSTV
LKDLKPETEY VVNVYSVVED EYSEPLKGTE KTLPVPVVSL NIYDVGPTTM HVQWQPVGGA
TGYILSYKPV KDTEPTRPKE VRLGPTVNDM QLTDLVPNTE YAVTVQAVLH DLTSEPVTVR
EVTLPLPRPQ DLKLRDVTHS TMNVFWEPVP GKVRKYIVRY KTPEEDVKEV EVDRSETSTS
LKDLFSQTLY TVSVSAVHDE GESPPVTAQE TTRPVPAPTN LKITEVTSEG FRGTWDHGAS
DVSLYRITWA PFGSSDKMET ILNGDENTLV FENLNPNTIY EVSITAIYPD ESESDDLIGS
ERTLPILTTQ APKSGPRNLQ VYNATSNSLT VKWDPASGRV QKYRITYQPS TGEGNEQTTT
IGGRQNSVVL QKLKPDTPYT ITVSSLYPDG EGGRMTGRGK TKPLNTVRNL RVYDPSTSTL
NVRWDHAEGN PRQYKLFYAP AAGGPEELVP IPGNTNYAIL RNLQPDTSYT VTVVPVYTEG
DGGRTSDTGR TLMRGLARNV QVYNPTPNSL DVRWDPAPGP VLQYRVVYSP VDGTRPSESI
VVPGNTRMVH LERLIPDTLY SVNLVALYSD GEGNPSPAQG RTLPRSGPRN LRVFGETTNS
LSVAWDHADG PVQQYRIIYS PTVGDPIDEY TTVPGRRNNV ILQPLQPDTP YKITVIAVYE
DGDGGHLTGN GRTVGLLPPQ NIHISDEWYT RFRVSWDPSP SPVLGYKIVY KPVGSNEPME
AFVGEMTSYT LHNLNPSTTY DVNVYAQYDS GLSVPLTDQG TTLYLNVTDL KTYQIGWDTF
CVKWSPHRAA TSYRLKLSPA DGTRGQEITV RGSETSHCFT GLSPDTDYGV TVFVQTPNLE
GPGVSVKEHT TVKPTEAPTE PPTPPPPPTI PPARDVCKGA KADIVFLTDA SWSIGDDNFN
KVVKFIFNTV GGFDEISPAG IQVSFVQYSD EVKSEFKLNT YNDKALALGA LQNIRYRGGN
TRTGKALTFI KEKVLTWESG MRKNVPKVLV VVTDGRSQDE VKKAALVIQQ SGFSVFVVGV
ADVDYNELAN IASKPSERHV FIVDDFESFE KIEDNLITFV CETATSSCPL IYLDGYTSPG
FKMLEAYNLT EKNFASVQGV SLESGSFPSY SAYRIQKNAF VNQPTADLHP NGLPPSYTII
LLFRLLPETP SDPFAIWQIT DRDYKPQVGV IADPSSKTLS FFNKDTRGEV QTVTFDTEEV
KTLFYGSFHK VHIVVTSKSV KIYIDCYEII EKDIKEAGNI TTDGYEILGK LLKGERKSAA
FQIQSFDIVC SPVWTSRDRC CDIPSRRDEG KCPAFPNSCT CTQDSVGPPG PPGPAGGPGA
KGPRGERGIS GAIGPPGPRG DIGPPGPQGP PGPQGPNGLS IPGEQGRQGM KGDAGEPGLP
GRTGTPGLPG PPGPMGPPGD RGFTGKDGAM GPRGPPGPPG SPGSPGVTGP SGKPGKPGDH
GRPGPSGLKG EKGDRGDIAS QNMMRAVARQ VCEQLISGQM NRFNQMLNQI PNDYQSSRNQ
PGPPGPPGPP GSAGARGEPG PGGRPGFPGT PGMQGPPGER GLPGEKGERG TGSSGPRGLP
GPPGPQGESR TGPPGSTGSR GPPGPPGRPG NSGIRGPPGP PGYCDSSQCA SIPYNGQGYP
GSG


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E0572h ELISA Alpha-1 type II collagen,COL2A1,Collagen alpha-1(II) chain,Homo sapiens,Human 96T
E0571h ELISA Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Homo sapiens,Human 96T
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E0571Rb ELISA Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Oryctolagus cuniculus,Rabbit 96T
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Pathways :
WP1614: 1- and 2-Methylnaphthalene degradation
WP1002: Electron Transport Chain
WP1883: Platelet Adhesion to exposed collagen
WP811: TNF-alpha NF-kB Signaling Pathway
WP1531: Vitamin D synthesis
WP263: Ovarian Infertility Genes
WP1584: Type II diabetes mellitus
WP296: TCA Cycle - biocyc
WP111: Electron Transport Chain
WP1996: Linoleate Biosynthesis
WP929: TNF-alpha NF-kB Signaling Pathway
WP1163: TNF-alpha NF-kB Signaling Pathway
WP215: noncanonical wnt pathway
WP1626: Benzoate degradation via CoA ligation
WP402: ERK1 - ERK2 MAPK cascade
WP1654: gamma-Hexachlorocyclohexane degradation
WP537: Translation Factors
WP1225: estrogen signalling
WP231: TNF alpha Signaling Pathway
WP1369: TNF-alpha NF-kB Signaling Pathway
WP2434: very-long-chain-fatty-acid-biosynthesis
WP1673: Naphthalene and anthracene degradation
WP59: Electron Transport Chain
WP1835: Interferon alpha/beta signaling
WP773: Ovarian Infertility Genes

Related Genes :
[COL12A1 COL12A1L] Collagen alpha-1(XII) chain
[Col12a1] Collagen alpha-1(XII) chain
[COL12A1] Collagen alpha-1(XII) chain (Fibrochimerin)
[COL19A1] Collagen alpha-1(XIX) chain (Collagen alpha-1(Y) chain)
[F12] Coagulation factor XII (EC 3.4.21.38) (Hageman factor) (HAF) [Cleaved into: Coagulation factor XIIa heavy chain; Beta-factor XIIa part 1; Coagulation factor XIIa light chain (Beta-factor XIIa part 2)]
[COL6A5 COL29A1 VWA4] Collagen alpha-5(VI) chain (Collagen alpha-1(XXIX) chain) (von Willebrand factor A domain-containing protein 4)
[COL7A1] Collagen alpha-1(VII) chain (Long-chain collagen) (LC collagen)
[COL1A1] Collagen alpha-1(I) chain (Alpha-1 type I collagen)
[Col1a1] Collagen alpha-1(I) chain (Alpha-1 type I collagen)
[Col1a1 Cola1] Collagen alpha-1(I) chain (Alpha-1 type I collagen)
[COL1A1] Collagen alpha-1(I) chain (Alpha-1 type I collagen)
[COL1A2] Collagen alpha-2(I) chain (Alpha-2 type I collagen)
[COL1A1] Collagen alpha-1(I) chain (Alpha-1 type I collagen)
[COL2A1] Collagen alpha-1(II) chain (Alpha-1 type II collagen) [Cleaved into: Collagen alpha-1(II) chain; Chondrocalcin]
[Col1a2] Collagen alpha-2(I) chain (Alpha-2 type I collagen)
[Col1a2 Cola2] Collagen alpha-2(I) chain (Alpha-2 type I collagen)
[COL2A1] Collagen alpha-1(II) chain (Alpha-1 type II collagen)
[COL1A1] Collagen alpha-1(I) chain (Alpha-1 type I collagen)
[COL1A2] Collagen alpha-2(I) chain (Alpha-2 type I collagen)
[Col4a1 Cg25C DCg1 CG4145] Collagen alpha-1(IV) chain (Collagen type IV alpha 1)
[COL1A2] Collagen alpha-2(I) chain (Alpha-2 type I collagen)
[Col2a1] Collagen alpha-1(II) chain (Alpha-1 type II collagen) [Cleaved into: Collagen alpha-1(II) chain; Chondrocalcin]
[Col2a1] Collagen alpha-1(II) chain (Alpha-1 type II collagen) [Cleaved into: Collagen alpha-1(II) chain; Chondrocalcin]
[COL2A1] Collagen alpha-1(II) chain (Alpha-1 type II collagen) (Fragment)
[COL26A1 EMID2 EMU2] Collagen alpha-1(XXVI) chain (Alpha-1 type XXVI collagen) (EMI domain-containing protein 2) (Emilin and multimerin domain-containing protein 2) (Emu2)
[Col26a1 Col26a Emid2 Emu2] Collagen alpha-1(XXVI) chain (Alpha-1 type XXVI collagen) (EMI domain-containing protein 2) (Emilin and multimerin domain-containing protein 2) (Emu2)
[COL8A1 C3orf7] Collagen alpha-1(VIII) chain (Endothelial collagen) [Cleaved into: Vastatin]
[COL25A1] Collagen alpha-1(XXV) chain (Alzheimer disease amyloid-associated protein) (AMY) (CLAC-P) [Cleaved into: Collagen-like Alzheimer amyloid plaque component (CLAC)]
[Col7a1] Collagen alpha-1(VII) chain (Long-chain collagen) (LC collagen)
[Col18a1] Collagen alpha-1(XVIII) chain [Cleaved into: Endostatin; Non-collagenous domain 1 (NC1)]

Bibliography :
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