Q07092 (COGA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-1(XVI) chain

Gene names

Name:	COL16A1
ORF Names:	FP1572

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1604 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology. Ref.11
Subunit structure	Homotrimer. Interacts with FBN1, fibronectin and integrins ITGA1/ITGB1 and ITGA2/ITGB1. Integrin ITGA1/ITGB1 binds to a unique site within COL16A1 located close to its C-terminal end between collagenous domains COL1-COL3. Ref.3 Ref.4 Ref.9 Ref.11
Subcellular location	Secreted › extracellular space › extracellular matrix Ref.9.
Tissue specificity	In papillary dermis, is a component of specialized fibrillin-1-containing microfibrils, whereas in territorial cartilage matrix, it is localized to a discrete population of thin, weakly banded collagen fibrils in association with other collagens (at protein level). In the placenta, where it is found in the amnion, a membranous tissue lining the amniotic cavity. Within the amnion, it is found in an acellular, relatively dense layer of a complex network of reticular fibers. Also located to a fibroblast layer beneath this dense layer. Exists in tissues in association with other types of collagen. Ref.10
Developmental stage	Transiently elevated expression during gestation, and decrease at term.
Domain	This sequence defines eighteen different domains, nine triple-helical domains (COL9 to COL1) and ten non-triple-helical domains (NC10 to NC1). The numerous interruptions in the triple helix may make this molecule either elastic or flexible.
Post-translational modification	Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. Glycosylated. Ref.3 Ref.4
Sequence similarities	Belongs to the fibril-associated collagens with interrupted helices (FACIT) family. Contains 8 collagen-like domains. Contains 1 laminin G-like domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Collagen Repeat Signal
PTM	Glycoprotein Hydroxylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from direct assay Ref.11. Source: UniProtKB cellular response to amino acid stimulus Inferred from electronic annotation. Source: Compara extracellular matrix organization Traceable author statement. Source: Reactome female pregnancy Traceable author statement Ref.7. Source: ProtInc integrin-mediated signaling pathway Traceable author statement Ref.11. Source: UniProtKB
Cellular_component	collagen type XVI Traceable author statement Ref.7. Source: ProtInc endoplasmic reticulum lumen Traceable author statement. Source: Reactome
Molecular_function	integrin binding Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q07092-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q07092-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1052-1052: Missing.
     1161-1161: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Ref.3 Ref.4
	Chain	22 – 1604	1583	Collagen alpha-1(XVI) chain		PRO_0000005792
Regions
	Domain	50 – 231	182	Laminin G-like
	Domain	375 – 423	49	Collagen-like 1
	Domain	573 – 633	61	Collagen-like 2
	Domain	667 – 721	55	Collagen-like 3
	Domain	788 – 840	53	Collagen-like 4
	Domain	888 – 938	51	Collagen-like 5
	Domain	1018 – 1075	58	Collagen-like 6
	Domain	1472 – 1524	53	Collagen-like 7
	Domain	1528 – 1576	49	Collagen-like 8
	Region	232 – 374	143	Nonhelical region 10 (NC10)
	Region	375 – 506	132	Triple-helical region 9 (COL9) with 3 imperfections
	Region	507 – 521	15	Nonhelical region 9 (NC9)
	Region	522 – 555	34	Triple-helical region 8 (COL8) with 1 imperfection
	Region	556 – 572	17	Nonhelical region 8 (NC8)
	Region	573 – 631	59	Triple-helical region 7 (COL7) with 1 imperfection
	Region	632 – 652	21	Nonhelical region 7 (NC7)
	Region	653 – 723	71	Triple-helical region 6 (COL6) with 1 imperfection
	Region	724 – 738	15	Nonhelical region 6 (NC6)
	Region	739 – 876	138	Triple-helical region 5 (COL5) with 3 imperfections
	Region	877 – 887	11	Nonhelical region 5 (NC5)
	Region	888 – 939	52	Triple-helical region 4 (COL4) with 2 imperfections
	Region	940 – 973	34	Nonhelical region 4 (NC4)
	Region	974 – 988	15	Triple-helical region 3 (COL3)
	Region	989 – 1011	23	Nonhelical region 3 (NC3)
	Region	1012 – 1433	422	Triple-helical region 2 (COL2) with 2 imperfections
	Region	1434 – 1472	39	Nonhelical region 2 (NC2)
	Region	1473 – 1578	106	Triple-helical region 1 (COL1) with 2 imperfections
	Region	1579 – 1604	26	Nonhelical region 1 (NC1)
	Motif	540 – 542	3	Cell attachment site Potential
	Motif	1006 – 1008	3	Cell attachment site Potential
	Motif	1227 – 1229	3	Cell attachment site Potential
Amino acid modifications
	Glycosylation	47	1	N-linked (GlcNAc...) Potential
	Glycosylation	327	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1052	1	Missing in isoform 2.		VSP_024259
	Alternative sequence	1161	1	Missing in isoform 2.		VSP_024260
	Natural variant	27	1	Q → H. Corresponds to variant rs2229802 [ dbSNP | Ensembl ].		VAR_048777
	Natural variant	62	1	T → K. Ref.1 Corresponds to variant rs2228552 [ dbSNP | Ensembl ].		VAR_031440
	Natural variant	418	1	R → Q. Corresponds to variant rs6699645 [ dbSNP | Ensembl ].		VAR_048778
	Natural variant	745	1	G → S. Corresponds to variant rs34770879 [ dbSNP | Ensembl ].		VAR_048779
	Natural variant	909	1	P → L. Corresponds to variant rs2229804 [ dbSNP | Ensembl ].		VAR_048780
Experimental info
	Sequence conflict	419	1	D → G in AAB25797. Ref.7
	Sequence conflict	420 – 421	2	GR → A in AAA58427. Ref.1
	Sequence conflict	538	1	P → R in AAA58427. Ref.1
	Sequence conflict	848 – 849	2	RD → VM in CAA33142. Ref.6
	Sequence conflict	848 – 849	2	RD → VM in CAA33085. Ref.6
	Sequence conflict	1161	1	P → T in AAA58427. Ref.1
	Sequence conflict	1164	1	P → T in AAA58427. Ref.1
	Sequence conflict	1166	1	P → S in AAA58427. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 3, 2007. Version 2. Checksum: 5FAA1950DFC6CA3C	FASTA	1,604	157,751
	10 20 30 40 50 60 MWVSWAPGLW LLGLWATFGH GANTGAQCPP SQQEGLKLEH SSSLPANVTG FNLIHRLSLM 70 80 90 100 110 120 KTSAIKKIRN PKGPLILRLG AAPVTQPTRR VFPRGLPEEF ALVLTLLLKK HTHQKTWYLF 130 140 150 160 170 180 QVTDANGYPQ ISLEVNSQER SLELRAQGQD GDFVSCIFPV PQLFDLRWHK LMLSVAGRVA 190 200 210 220 230 240 SVHVDCSSAS SQPLGPRRPM RPVGHVFLGL DAEQGKPVSF DLQQVHIYCD PELVLEEGCC 250 260 270 280 290 300 EILPAGCPPE TSKARRDTQS NELIEINPQS EGKVYTRCFC LEEPQNSEVD AQLTGRISQK 310 320 330 340 350 360 AERGAKVHQE TAADECPPCV HGARDSNVTL APSGPKGGKG ERGLPGPPGS KGEKGARGND 370 380 390 400 410 420 CVRISPDAPL QCAEGPKGEK GESGALGPSG LPGSTGEKGQ KGEKGDGGIK GVPGKPGRDG 430 440 450 460 470 480 RPGEICVIGP KGQKGDPGFV GPEGLAGEPG PPGLPGPPGI GLPGTPGDPG GPPGPKGDKG 490 500 510 520 530 540 SSGIPGKEGP GGKPGKPGVK GEKGDPCEVC PTLPEGFQNF VGLPGKPGPK GEPGDPVPAR 550 560 570 580 590 600 GDPGIQGIKG EKGEPCLSCS SVVGAQHLVS STGASGDVGS PGFGLPGLPG RAGVPGLKGE 610 620 630 640 650 660 KGNFGEAGPA GSPGPPGPVG PAGIKGAKGE PCEPCPALSN LQDGDVRVVA LPGPSGEKGE 670 680 690 700 710 720 PGPPGFGLPG KQGKAGERGL KGQKGDAGNP GDPGTPGTTG RPGLSGEPGV QGPAGPKGEK 730 740 750 760 770 780 GDGCTACPSL QGTVTDMAGR PGQPGPKGEQ GPEGVGRPGK PGQPGLPGVQ GPPGLKGVQG 790 800 810 820 830 840 EPGPPGRGVQ GPQGEPGAPG LPGIQGLPGP RGPPGPTGEK GAQGSPGVKG ATGPVGPPGA 850 860 870 880 890 900 SVSGPPGRDG QQGQTGLRGT PGEKGPRGEK GEPGECSCPS QGDLIFSGMP GAPGLWMGSS 910 920 930 940 950 960 WQPGPQGPPG IPGPPGPPGV PGLQGVPGNN GLPGQPGLTA ELGSLPIEQH LLKSICGDCV 970 980 990 1000 1010 1020 QGQRAHPGYL VEKGEKGDQG IPGVPGLDNC AQCFLSLERP RAEEARGDNS EGDPGCVGSP 1030 1040 1050 1060 1070 1080 GLPGPPGLPG QRGEEGPPGM RGSPGPPGPI GPPGFPGAVG SPGLPGLQGE RGLTGLTGDK 1090 1100 1110 1120 1130 1140 GEPGPPGQPG YPGATGPPGL PGIKGERGYT GSAGEKGEPG PPGSEGLPGP PGPAGPRGER 1150 1160 1170 1180 1190 1200 GPQGNSGEKG DQGFQGQPGF PGPPGPPGFP GKVGSPGPPG PQAEKGSEGI RGPSGLPGSP 1210 1220 1230 1240 1250 1260 GPPGPPGIQG PAGLDGLDGK DGKPGLRGDP GPAGPPGLMG PPGFKGKTGH PGLPGPKGDC 1270 1280 1290 1300 1310 1320 GKPGPPGSTG RPGAEGEPGA MGPQGRPGPP GHVGPPGPPG QPGPAGISAV GLKGDRGATG 1330 1340 1350 1360 1370 1380 ERGLAGLPGQ PGPPGHPGPP GEPGTDGAAG KEGPPGKQGF YGPPGPKGDP GAAGQKGQAG 1390 1400 1410 1420 1430 1440 EKGRAGMPGG PGKSGSMGPV GPPGPAGERG HPGAPGPSGS PGLPGVPGSM GDMVNYDEIK 1450 1460 1470 1480 1490 1500 RFIRQEIIKM FDERMAYYTS RMQFPMEMAA APGRPGPPGK DGAPGRPGAP GSPGLPGQIG 1510 1520 1530 1540 1550 1560 REGRQGLPGV RGLPGTKGEK GDIGIGIAGE NGLPGPPGPQ GPPGYGKMGA TGPMGQQGIP 1570 1580 1590 1600 GIPGPPGPMG QPGKAGHCNP SDCFGAMPME QQYPPMKTMK GPFG
	Isoform 2 [UniParc]. Checksum: C0F8388B57BBA080	FASTA	1,602	157,557
	10 20 30 40 50 60 MWVSWAPGLW LLGLWATFGH GANTGAQCPP SQQEGLKLEH SSSLPANVTG FNLIHRLSLM 70 80 90 100 110 120 KTSAIKKIRN PKGPLILRLG AAPVTQPTRR VFPRGLPEEF ALVLTLLLKK HTHQKTWYLF 130 140 150 160 170 180 QVTDANGYPQ ISLEVNSQER SLELRAQGQD GDFVSCIFPV PQLFDLRWHK LMLSVAGRVA 190 200 210 220 230 240 SVHVDCSSAS SQPLGPRRPM RPVGHVFLGL DAEQGKPVSF DLQQVHIYCD PELVLEEGCC 250 260 270 280 290 300 EILPAGCPPE TSKARRDTQS NELIEINPQS EGKVYTRCFC LEEPQNSEVD AQLTGRISQK 310 320 330 340 350 360 AERGAKVHQE TAADECPPCV HGARDSNVTL APSGPKGGKG ERGLPGPPGS KGEKGARGND 370 380 390 400 410 420 CVRISPDAPL QCAEGPKGEK GESGALGPSG LPGSTGEKGQ KGEKGDGGIK GVPGKPGRDG 430 440 450 460 470 480 RPGEICVIGP KGQKGDPGFV GPEGLAGEPG PPGLPGPPGI GLPGTPGDPG GPPGPKGDKG 490 500 510 520 530 540 SSGIPGKEGP GGKPGKPGVK GEKGDPCEVC PTLPEGFQNF VGLPGKPGPK GEPGDPVPAR 550 560 570 580 590 600 GDPGIQGIKG EKGEPCLSCS SVVGAQHLVS STGASGDVGS PGFGLPGLPG RAGVPGLKGE 610 620 630 640 650 660 KGNFGEAGPA GSPGPPGPVG PAGIKGAKGE PCEPCPALSN LQDGDVRVVA LPGPSGEKGE 670 680 690 700 710 720 PGPPGFGLPG KQGKAGERGL KGQKGDAGNP GDPGTPGTTG RPGLSGEPGV QGPAGPKGEK 730 740 750 760 770 780 GDGCTACPSL QGTVTDMAGR PGQPGPKGEQ GPEGVGRPGK PGQPGLPGVQ GPPGLKGVQG 790 800 810 820 830 840 EPGPPGRGVQ GPQGEPGAPG LPGIQGLPGP RGPPGPTGEK GAQGSPGVKG ATGPVGPPGA 850 860 870 880 890 900 SVSGPPGRDG QQGQTGLRGT PGEKGPRGEK GEPGECSCPS QGDLIFSGMP GAPGLWMGSS 910 920 930 940 950 960 WQPGPQGPPG IPGPPGPPGV PGLQGVPGNN GLPGQPGLTA ELGSLPIEQH LLKSICGDCV 970 980 990 1000 1010 1020 QGQRAHPGYL VEKGEKGDQG IPGVPGLDNC AQCFLSLERP RAEEARGDNS EGDPGCVGSP 1030 1040 1050 1060 1070 1080 GLPGPPGLPG QRGEEGPPGM RGSPGPPGPI GPGFPGAVGS PGLPGLQGER GLTGLTGDKG 1090 1100 1110 1120 1130 1140 EPGPPGQPGY PGATGPPGLP GIKGERGYTG SAGEKGEPGP PGSEGLPGPP GPAGPRGERG 1150 1160 1170 1180 1190 1200 PQGNSGEKGD QGFQGQPGFG PPGPPGFPGK VGSPGPPGPQ AEKGSEGIRG PSGLPGSPGP 1210 1220 1230 1240 1250 1260 PGPPGIQGPA GLDGLDGKDG KPGLRGDPGP AGPPGLMGPP GFKGKTGHPG LPGPKGDCGK 1270 1280 1290 1300 1310 1320 PGPPGSTGRP GAEGEPGAMG PQGRPGPPGH VGPPGPPGQP GPAGISAVGL KGDRGATGER 1330 1340 1350 1360 1370 1380 GLAGLPGQPG PPGHPGPPGE PGTDGAAGKE GPPGKQGFYG PPGPKGDPGA AGQKGQAGEK 1390 1400 1410 1420 1430 1440 GRAGMPGGPG KSGSMGPVGP PGPAGERGHP GAPGPSGSPG LPGVPGSMGD MVNYDEIKRF 1450 1460 1470 1480 1490 1500 IRQEIIKMFD ERMAYYTSRM QFPMEMAAAP GRPGPPGKDG APGRPGAPGS PGLPGQIGRE 1510 1520 1530 1540 1550 1560 GRQGLPGVRG LPGTKGEKGD IGIGIAGENG LPGPPGPQGP PGYGKMGATG PMGQQGIPGI 1570 1580 1590 1600 PGPPGPMGQP GKAGHCNPSD CFGAMPMEQQ YPPMKTMKGP FG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and chromosomal location of human alpha 1(XVI) collagen." Pan T.-C., Zhang R.-Z., Mattei M.-G., Timpl R., Chu M.-L. Proc. Natl. Acad. Sci. U.S.A. 89:6565-6569(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-62. Tissue: Fibroblast.
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Recombinant analysis of human alpha 1 (XVI) collagen. Evidence for processing of the N-terminal globular domain." Tillet E., Mann K., Nischt R., Pan T.-C., Chu M.-L., Timpl R. Eur. J. Biochem. 228:160-168(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-33, SUBUNIT, GLYCOSYLATION.
[4]	"Molecular structure and interaction of recombinant human type XVI collagen." Kassner A., Tiedemann K., Notbohm H., Ludwig T., Morgelin M., Reinhardt D.P., Chu M.-L., Bruckner P., Grassel S. J. Mol. Biol. 339:835-853(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-30; 257-265 AND 941-950, SUBUNIT, INTERACTION WITH FBN1 AND FN1, GLYCOSYLATION.
[5]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-1604 (ISOFORM 2). Tissue: Spleen.
[6]	Kimura S. Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 403-849. Tissue: Placenta.
[7]	"Molecular cloning and partial characterization of a novel collagen chain, alpha 1(XVI), consisting of repetitive collagenous domains and cysteine-containing non-collagenous segments." Yamaguchi N., Kimura S., McBride O.W., Hori H., Yamada Y., Kanamori T., Yamakoshi H., Nagai Y. J. Biochem. 112:856-863(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 418-1604 (ISOFORM 1). Tissue: Placenta.
[8]	"Large-scale cDNA transfection screening for genes related to cancer development and progression." Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J. Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1387-1604.
[9]	"Biosynthesis and processing of type XVI collagen in human fibroblasts and smooth muscle cells." Grassel S., Timpl R., Tan E.M.L., Chu M.-L. Eur. J. Biochem. 242:576-584(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[10]	"Discrete integration of collagen XVI into tissue-specific collagen fibrils or beaded microfibrils." Kassner A., Hansen U., Miosge N., Reinhardt D.P., Aigner T., Bruckner-Tuderman L., Bruckner P., Grassel S. Matrix Biol. 22:131-143(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[11]	"Collagen XVI harbors an integrin alpha1 beta1 recognition site in its C-terminal domains." Eble J.A., Kassner A., Niland S., Morgelin M., Grifka J., Grassel S. J. Biol. Chem. 281:25745-25756(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, INTERACTION WITH INTEGRIN ALPHA-1/BETA-1 AND INTEGRIN ALPHA-2/BETA-1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M92642 mRNA. Translation: AAA58427.1. AC114488 Genomic DNA. No translation available. AB209571 mRNA. Translation: BAD92808.1. X14963 mRNA. Translation: CAA33085.1. X15038 mRNA. Translation: CAA33142.1. S57132 mRNA. Translation: AAB25797.1. AF370368 mRNA. Translation: AAQ15204.1.
IPI	IPI00400935. IPI00641471.
PIR	S23810.
RefSeq	NP_001847.3. NM_001856.3.
UniGene	Hs.368921.
3D structure databases
ProteinModelPortal	Q07092.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q07092. 1 interaction.
MINT	MINT-6743139.
STRING	9606.ENSP00000362776.
PTM databases
PhosphoSite	Q07092.
Polymorphism databases
DMDM	143811380.
Proteomic databases
PaxDb	Q07092.
PRIDE	Q07092.
Protocols and materials databases
DNASU	1307.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000373672; ENSP00000362776; ENSG00000084636.
GeneID	1307.
KEGG	hsa:1307.
UCSC	uc001btj.1. human. uc001btk.1. human.
Organism-specific databases
CTD	1307.
GeneCards	GC01M032117.
H-InvDB	HIX0028602.
HGNC	HGNC:2193. COL16A1.
HPA	HPA027235. HPA027237.
MIM	120326. gene.
neXtProt	NX_Q07092.
PharmGKB	PA26709.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOGENOM	HOG000085653.
HOVERGEN	HBG071631.
InParanoid	Q07092.
OMA	CEVCPTL.
OrthoDB	EOG47WNN3.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	Q07092.
Bgee	Q07092.
CleanEx	HS_COL16A1.
Genevestigator	Q07092.
GermOnline	ENSG00000084636. Homo sapiens.
Family and domain databases
InterPro	IPR008160. Collagen. IPR008985. ConA-like_lec_gl_sf. IPR001791. Laminin_G. [Graphical view]
Pfam	PF01391. Collagen. 8 hits. [Graphical view]
SMART	SM00210. TSPN. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS50025. LAM_G_DOMAIN. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1307.
NextBio	5349.
SOURCE	Search...

Entry information

Entry name

COGA1_HUMAN

Accession

Primary (citable) accession number: Q07092
Secondary accession number(s): Q16593, Q59F89, Q71RG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	April 3, 2007
Last modified:	May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.