P05997 (CO5A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-2(V) chain

Gene names

Name:

COL5A2

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	1499 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	Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specific matrices By similarity.
Subunit structure	Trimers of two alpha 1(V) and one alpha 2(V) chains in most tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha 3(V) chains in placenta.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Domain	The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function By similarity.
Post-translational modification	Prolines at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Probably 3-hydroxylated on Pro-919 and Pro-1156 by LEPREL1.
Involvement in disease	Ehlers-Danlos syndrome 1 (EDS1) [MIM:130000]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ehlers-Danlos syndrome 2 (EDS2) [MIM:130010]: Mild form of classic Ehlers-Danlos syndrome. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17
Sequence similarities	Belongs to the fibrillar collagen family. Contains 1 fibrillar collagen NC1 domain. Contains 1 VWFC domain.
Sequence caution	The sequence AAH43613.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAY24185.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAD92282.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation Ehlers-Danlos syndrome
Domain	Collagen Repeat Signal
Ligand	Calcium Metal-binding
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome cellular response to amino acid stimulus Inferred from electronic annotation. Source: Compara collagen catabolic process Traceable author statement. Source: Reactome collagen fibril organization Inferred from mutant phenotype Ref.15. Source: UniProtKB extracellular matrix disassembly Traceable author statement. Source: Reactome eye morphogenesis Inferred from mutant phenotype PubMed 16431952. Source: UniProtKB skeletal system development Inferred from electronic annotation. Source: Compara skin development Inferred from mutant phenotype Ref.15. Source: UniProtKB
Cellular_component	collagen type V Inferred from mutant phenotype Ref.15Ref.17. Source: UniProtKB endoplasmic reticulum lumen Traceable author statement. Source: Reactome
Molecular_function	extracellular matrix structural constituent Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26
	Chain	27 – 1229	1203	Collagen alpha-2(V) chain		PRO_0000005830
	Propeptide	1230 – 1499	270	C-terminal propeptide		PRO_0000005831
Regions
	Domain	39 – 97	59	VWFC
	Domain	1266 – 1499	234	Fibrillar collagen NC1
	Motif	506 – 508	3	Cell attachment site Potential
	Motif	944 – 946	3	Cell attachment site Potential
	Motif	1067 – 1069	3	Cell attachment site Potential
	Motif	1070 – 1072	3	Cell attachment site Potential
	Motif	1100 – 1102	3	Cell attachment site Potential
	Motif	1127 – 1129	3	Cell attachment site Potential
	Motif	1136 – 1138	3	Cell attachment site Potential
Sites
	Metal binding	1314	1	Calcium By similarity
	Metal binding	1316	1	Calcium By similarity
	Metal binding	1317	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	1322	1	Calcium By similarity
Amino acid modifications
	Modified residue	290	1	Hydroxyproline
	Modified residue	293	1	Hydroxyproline
	Modified residue	296	1	Hydroxyproline
	Modified residue	611	1	Hydroxyproline
	Modified residue	617	1	Hydroxyproline
	Modified residue	919	1	3-hydroxyproline; partial Ref.16
	Modified residue	1156	1	3-hydroxyproline; partial Ref.16
	Glycosylation	1262	1	N-linked (GlcNAc...) Potential
	Glycosylation	1400	1	N-linked (GlcNAc...) Potential
	Disulfide bond	1296 ↔ 1328		By similarity
	Disulfide bond	1336 ↔ 1497		By similarity
	Disulfide bond	1405 ↔ 1450		By similarity
Natural variations
	Natural variant	460	1	P → S. Corresponds to variant rs35830636 [ dbSNP | Ensembl ].		VAR_048799
	Natural variant	512	1	V → A. Ref.18 Corresponds to variant rs35852101 [ dbSNP | Ensembl ].		VAR_057910
	Natural variant	833	1	P → L. Ref.18		VAR_057911
	Natural variant	956	1	R → P. Corresponds to variant rs6434313 [ dbSNP | Ensembl ].		VAR_048800
	Natural variant	963	1	G → R in EDS2. Ref.17		VAR_013588
	Natural variant	1230	1	T → S. Ref.18		VAR_057912
	Natural variant	1432	1	D → V. Ref.18		VAR_057913
Experimental info
	Sequence conflict	292	1	A → P AA sequence Ref.8
	Sequence conflict	361	1	M → L in AAL13166. Ref.5
	Sequence conflict	430	1	A → P in CAA75002. Ref.1
	Sequence conflict	430	1	A → P in AAA51859. Ref.4
	Sequence conflict	430	1	A → P in CAA28454. Ref.9
	Sequence conflict	463 – 466	4	IRGQ → NSGL in CAA75002. Ref.1
	Sequence conflict	463 – 466	4	IRGQ → NSGL in CAA28454. Ref.9
	Sequence conflict	463	1	I → N in AAA51859. Ref.4
	Sequence conflict	472 – 474	3	Missing in CAA75002. Ref.1
	Sequence conflict	472 – 474	3	Missing in CAA28454. Ref.9
	Sequence conflict	512	1	V → L in CAA75002. Ref.1
	Sequence conflict	512	1	V → L in CAA28454. Ref.9
	Sequence conflict	608	1	R → K in CAA75002. Ref.1
	Sequence conflict	608	1	R → K in CAA28454. Ref.9
	Sequence conflict	613	1	S → T in CAA75002. Ref.1
	Sequence conflict	613	1	S → T in CAA28454. Ref.9
	Sequence conflict	623	1	S → N in CAA75002. Ref.1
	Sequence conflict	623	1	S → N in CAA28454. Ref.9
	Sequence conflict	635	1	A → P in CAA75002. Ref.1
	Sequence conflict	635	1	A → P in CAA28454. Ref.9
	Sequence conflict	649	1	E → K in CAA75002. Ref.1
	Sequence conflict	649	1	E → K in CAA28454. Ref.9
	Sequence conflict	653	1	S → Y in CAA75002. Ref.1
	Sequence conflict	653	1	S → Y in CAA28454. Ref.9
	Sequence conflict	656	1	V → P in CAA75002. Ref.1
	Sequence conflict	656	1	V → P in CAA28454. Ref.9
	Sequence conflict	662	1	A → R in CAA75002. Ref.1
	Sequence conflict	662	1	A → R in CAA28454. Ref.9
	Sequence conflict	679	1	L → H in CAA75002. Ref.1
	Sequence conflict	679	1	L → H in CAA28454. Ref.9
	Sequence conflict	700	1	D → G in CAA75002. Ref.1
	Sequence conflict	700	1	D → G in CAA28454. Ref.9
	Sequence conflict	797	1	R → G in CAA75002. Ref.1
	Sequence conflict	797	1	R → G in CAA28454. Ref.9
	Sequence conflict	811 – 812	2	PT → LL in CAA75002. Ref.1
	Sequence conflict	811 – 812	2	PT → LL in CAA28454. Ref.9
	Sequence conflict	853	1	P → S in CAA75002. Ref.1
	Sequence conflict	853	1	P → S in CAA28454. Ref.9
	Sequence conflict	943	1	L → P in CAA75002. Ref.1
	Sequence conflict	943	1	L → P in CAA28454. Ref.9
	Sequence conflict	955	1	D → V in CAA75002. Ref.1
	Sequence conflict	955	1	D → V in CAA28454. Ref.9
	Sequence conflict	1111 – 1112	2	PP → HL in CAA75002. Ref.1
	Sequence conflict	1111 – 1112	2	PP → HL in CAA28454. Ref.9
	Sequence conflict	1111 – 1112	2	PP → HL in AAA52007. Ref.11
	Sequence conflict	1196	1	I → L in CAA75002. Ref.1
	Sequence conflict	1196	1	I → L in CAA28454. Ref.9
	Sequence conflict	1196	1	I → L in AAA52007. Ref.11
	Sequence conflict	1421	1	K → T in AAA52058. Ref.13
	Sequence conflict	1441	1	F → S in AAA52058. Ref.13
	Sequence conflict	1467	1	Q → E in AAA51858. Ref.14

Sequences

	Sequence		Length	Mass (Da)
	P05997 [UniParc]. Last modified April 3, 2007. Version 3. Checksum: E8C92BF5E749EC97	FASTA	1,499	144,910
	10 20 30 40 50 60 MMANWAEARP LLILIVLLGQ FVSIKAQEED EDEGYGEEIA CTQNGQMYLN RDIWKPAPCQ 70 80 90 100 110 120 ICVCDNGAIL CDKIECQDVL DCADPVTPPG ECCPVCSQTP GGGNTNFGRG RKGQKGEPGL 130 140 150 160 170 180 VPVVTGIRGR PGPAGPPGSQ GPRGERGPKG RPGPRGPQGI DGEPGVPGQP GAPGPPGHPS 190 200 210 220 230 240 HPGPDGLSRP FSAQMAGLDE KSGLGSQVGL MPGSVGPVGP RGPQGLQGQQ GGAGPTGPPG 250 260 270 280 290 300 EPGDPGPMGP IGSRGPEGPP GKPGEDGEPG RNGNPGEVGF AGSPGARGFP GAPGLPGLKG 310 320 330 340 350 360 HRGHKGLEGP KGEVGAPGSK GEAGPTGPMG AMGPLGPRGM PGERGRLGPQ GAPGQRGAHG 370 380 390 400 410 420 MPGKPGPMGP LGIPGSSGFP GNPGMKGEAG PTGARGPEGP QGQRGETGPP GPVGSPGLPG 430 440 450 460 470 480 AIGTDGTPGA KGPTGSPGTS GPPGSAGPPG SPGPQGSTGP QGIRGQPGDP GVPGFKGEAG 490 500 510 520 530 540 PKGEPGPHGI QGPIGPPGEE GKRGPRGDPG TVGPPGPVGE RGAPGNRGFP GSDGLPGPKG 550 560 570 580 590 600 AQGERGPVGS SGPKGSQGDP GRPGEPGLPG ARGLTGNPGV QGPEGKLGPL GAPGEDGRPG 610 620 630 640 650 660 PPGSIGIRGQ PGSMGLPGPK GSSGDPGKPG EAGNAGVPGQ RGAPGKDGEV GPSGPVGPPG 670 680 690 700 710 720 LAGERGEQGP PGPTGFQGLP GPPGPPGEGG KPGDQGVPGD PGAVGPLGPR GERGNPGERG 730 740 750 760 770 780 EPGITGLPGE KGMAGGHGPD GPKGSPGPSG TPGDTGPPGL QGMPGERGIA GTPGPKGDRG 790 800 810 820 830 840 GIGEKGAEGT AGNDGARGLP GPLGPPGPAG PTGEKGEPGP RGLVGPPGSR GNPGSRGENG 850 860 870 880 890 900 PTGAVGFAGP QGPDGQPGVK GEPGEPGQKG DAGSPGPQGL AGSPGPHGPN GVPGLKGGRG 910 920 930 940 950 960 TQGPPGATGF PGSAGRVGPP GPAGAPGPAG PLGEPGKEGP PGLRGDPGSH GRVGDRGPAG 970 980 990 1000 1010 1020 PPGGPGDKGD PGEDGQPGPD GPPGPAGTTG QRGIVGMPGQ RGERGMPGLP GPAGTPGKVG 1030 1040 1050 1060 1070 1080 PTGATGDKGP PGPVGPPGSN GPVGEPGPEG PAGNDGTPGR DGAVGERGDR GDPGPAGLPG 1090 1100 1110 1120 1130 1140 SQGAPGTPGP VGAPGDAGQR GDPGSRGPIG PPGRAGKRGL PGPQGPRGDK GDHGDRGDRG 1150 1160 1170 1180 1190 1200 QKGHRGFTGL QGLPGPPGPN GEQGSAGIPG PFGPRGPPGP VGPSGKEGNP GPLGPIGPPG 1210 1220 1230 1240 1250 1260 VRGSVGEAGP EGPPGEPGPP GPPGPPGHLT AALGDIMGHY DESMPDPLPE FTEDQAAPDD 1270 1280 1290 1300 1310 1320 KNKTDPGVHA TLKSLSSQIE TMRSPDGSKK HPARTCDDLK LCHSAKQSGE YWIDPNQGSV 1330 1340 1350 1360 1370 1380 EDAIKVYCNM ETGETCISAN PSSVPRKTWW ASKSPDNKPV WYGLDMNRGS QFAYGDHQSP 1390 1400 1410 1420 1430 1440 NTAITQMTFL RLLSKEASQN ITYICKNSVG YMDDQAKNLK KAVVLKGAND LDIKAEGNIR 1450 1460 1470 1480 1490 FRYIVLQDTC SKRNGNVGKT VFEYRTQNVA RLPIIDLAPV DVGGTDQEFG VEIGPVCFV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Richards A.J. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	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]. Tissue: Brain.
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Amino-terminal propeptide of human pro-alpha 2(V) collagen conforms to the structural criteria of a fibrillar procollagen molecule." Woodbury D., Benson-Chanda V., Ramirez F. J. Biol. Chem. 264:2735-2738(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-463.
[5]	"Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2 has evolved differently than the other minor fibrillar collagen genes." Valkkila M., Melkoniemi M., Kvist L., Kuivaniemi H., Tromp G., Ala-Kokko L. Matrix Biol. 20:357-366(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104 AND 153-1499.
[6]	"Homology between alpha 2(V) and alpha 1(III) collagen promoters and evidence for negatively acting elements in the alpha 2(V) first intron and 5' flanking sequences." Greenspan D.S., Lee S.T., Lee B.S., Hoffman G.G. Gene Expr. 1:29-39(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
[7]	"Isolation of the alpha 3-chain of human type V collagen and characterization by partial sequencing." Mann K. Biol. Chem. Hoppe-Seyler 373:69-75(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 208-227. Tissue: Placenta.
[8]	"Diversity in the processing events at the N-terminus of type-V collagen." Moradi-Ameli M., Rousseau J.C., Kleman J.P., Champliaud M.-F., Boutillon M.-M., Bernillon J., Wallach J.M., van der Rest M. Eur. J. Biochem. 221:987-995(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 288-297 AND 609-620. Tissue: Bone.
[9]	"The pro alpha 2(V) collagen gene is evolutionarily related to the major fibrillar-forming collagens." Weil D., Bernard M.P., Gargano S., Ramirez F. Nucleic Acids Res. 15:181-198(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 398-1499.
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 878-1499. Tissue: Skin.
[11]	"Partial covalent structure of the human alpha 2 type V collagen chain." Myers J.C., Loidl H.R., Stolle C.A., Seyer J.M. J. Biol. Chem. 260:5533-5541(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1005-1229, PROTEIN SEQUENCE OF 1006-1036.
[12]	"Human alpha 1(III) and alpha 2(V) procollagen genes are located on the long arm of chromosome 2." Emanuel B.S., Cannizzaro L.A., Seyer J.M., Myers J.C. Proc. Natl. Acad. Sci. U.S.A. 82:3385-3389(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1006-1037.
[13]	"Complete primary structure of the human alpha 2 type V procollagen COOH-terminal propeptide." Myers J.C., Loidl H.R., Seyer J.M., Dion A.S. J. Biol. Chem. 260:11216-11222(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1230-1499.
[14]	"Genetic distance of two fibrillar collagen loci, COL3A1 and COL5A2, located on the long arm of human chromosome 2." Tsipouras P., Schwartz R.C., Liddell A.C., Salkeld C.S., Weil D., Ramirez F. Genomics 3:275-277(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1452-1499.
[15]	"Mutations of the alpha2(V) chain of type V collagen impair matrix assembly and produce Ehlers-Danlos syndrome type I." Michalickova K., Susic M., Willing M.C., Wenstrup R.J., Cole W.G. Hum. Mol. Genet. 7:249-255(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN EDS1.
[16]	"A role for prolyl 3-hydroxylase 2 in post-translational modification of fibril-forming collagens." Fernandes R.J., Farnand A.W., Traeger G.R., Weis M.A., Eyre D.R. J. Biol. Chem. 286:30662-30669(2011) [PubMed] [Europe PMC] [Abstract] Cited for: HYDROXYLATION AT PRO-919 AND PRO-1156, MASS SPECTROMETRY.
[17]	"A single base mutation in COL5A2 causes Ehlers-Danlos syndrome type II." Richards A.J., Martin S., Nicholls A.C., Harrison J.B., Pope F.M., Burrows N.P. J. Med. Genet. 35:846-848(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT EDS2 ARG-963.
[18]	"Sequence analysis of the COL5A2 gene in patients with spontaneous cervical artery dissections." Grond-Ginsbach C., Wigger F., Morcher M., von Pein F., Grau A., Hausser I., Brandt T. Neurology 58:1103-1105(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ALA-512; LEU-833; SER-1230 AND VAL-1432.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y14690 mRNA. Translation: CAA75002.1.
AB209045 mRNA. Translation: BAD92282.1. Different initiation.
AC064833 Genomic DNA. No translation available.
AC133106 Genomic DNA. Translation: AAY24185.1. Sequence problems.
J04478 mRNA. Translation: AAA51859.1.
AY016288, AY016287 Genomic DNA. Translation: AAL13165.1.
AY016295 , AY016289, AY016290, AY016291, AY016292, AY016293, AY016294 Genomic DNA. Translation: AAL13166.1.
M58529 Genomic DNA. Translation: AAC41699.1.
X04758 mRNA. Translation: CAA28454.1.
BC043613 mRNA. Translation: AAH43613.1. Different initiation.
M10956 mRNA. Translation: AAA52007.1.
M11135 mRNA. Translation: AAA51857.1.
M11718 mRNA. Translation: AAA52058.1.
J03051 Genomic DNA. Translation: AAA51858.1.

IPI

IPI00739099.

PIR

CGHU2V. A31427.

RefSeq

NP_000384.2. NM_000393.3.

UniGene

Hs.445827.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A9A	model	-	B	561-581	[»]

ProteinModelPortal

P05997.

ModBase

Search...

PTM databases

PhosphoSite

P05997.

Polymorphism databases

DMDM

143811378.

Proteomic databases

PaxDb

P05997.

PRIDE

P05997.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374866; ENSP00000364000; ENSG00000204262.

GeneID

1290.

KEGG

hsa:1290.

UCSC

uc002uqk.3. human.

Organism-specific databases

CTD

1290.

GeneCards

GC02M189861.

HGNC

HGNC:2210. COL5A2.

MIM

120190. gene.
130000. phenotype.
130010. phenotype.

neXtProt

NX_P05997.

Orphanet

90309. Ehlers-Danlos syndrome type 1.
90318. Ehlers-Danlos syndrome type 2.

PharmGKB

PA26725.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOVERGEN

HBG004933.

InParanoid

P05997.

KO

K06236.

OMA

PDHKPVW.

OrthoDB

EOG4K0QMS.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpress

P05997.

Bgee

P05997.

Genevestigator

P05997.

GermOnline

ENSG00000204262. Homo sapiens.

Family and domain databases

InterPro

IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]

Pfam

PF01410. COLFI. 1 hit.
PF01391. Collagen. 9 hits.
PF00093. VWC. 1 hit.
[Graphical view]

ProDom

PD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]

PROSITE

PS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

COL5A2. human.

GenomeRNAi

1290.

NextBio

5223.

PMAP-CutDB

P05997.

SOURCE

Search...

Entry information

Entry name

CO5A2_HUMAN

Accession

Primary (citable) accession number: P05997
Secondary accession number(s): P78440 , Q13908, Q53WR4, Q59GR4, Q6LDJ5, Q7KZ55, Q86XF6, Q96QB0, Q96QB3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 3, 2007
Last modified:	May 29, 2013
This is version 151 of the entry and version 3 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.