Q3U962 (CO5A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-2(V) chain

Gene names

Name:

Col5a2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1497 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. Ref.1 Ref.4 Ref.5 UniProtKB P05997
Subunit structure	Trimers of two alpha 1(V) and one alpha 2(V) chains expressed in most tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha 3(V) chains with a more limited distribution of expression. Ref.6 UniProtKB P05997
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Developmental stage	Expressed in embryos from 9 days of gestation onward. In 12.5 dpc embryos, low and diffuse level of expression was observed in the peritoneal membranes and intestinal and craniofacial mesenchymes. By 16.5 dpc, expression is higher and exhibits a more restricted accumulation in primary ossified regions, perichondrium, joints, tendon, atrioventricular valve of heart, and in selected portions of the head. Ref.1
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 prolines by LEPREL1. UniProtKB P05997 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 By similarity.
Miscellaneous	Mice homozygous for the targeted deletion of the N-terminal telopeptide segment of the COL5A2 chain show poor survival rates, possibly because of complications from spinal deformities, and exhibit skin and eye abnormalities caused by disorganized type I collagen fibrils. Ref.4 Ref.5 Ref.6 The alpha 1(V)-alpha 1(V)-alpha 2(V) heterotrimer makes a critical contribution to fibrillogenesis, basement membrane organization, and cell viability, and may play a possible role in the development of a functional skin matrix. Ref.6
Sequence similarities	Belongs to the fibrillar collagen family. Contains 1 fibrillar collagen NC1 domain. Contains 1 VWFC domain.
Sequence caution	The sequence BAE23896.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Domain	Collagen Repeat Signal
Ligand	Calcium Metal-binding
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to amino acid stimulus Inferred from direct assay PubMed 20548288. Source: MGI collagen fibril organization Inferred from mutant phenotype Ref.6. Source: UniProtKB eye morphogenesis Inferred from electronic annotation. Source: Compara skeletal system development Inferred from mutant phenotype Ref.4. Source: MGI skin development Inferred from mutant phenotype Ref.6. Source: UniProtKB
Cellular_component	collagen Inferred from direct assay Ref.4. Source: MGI collagen type V Inferred from electronic annotation. Source: Compara
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	Potential
	Chain	27 – 1227	1201	Collagen alpha-2(V) chain		PRO_0000283768
	Propeptide	1228 – 1497	270	C-terminal propeptide		PRO_0000283769
Regions
	Domain	38 – 96	59	VWFC
	Domain	1264 – 1497	234	Fibrillar collagen NC1
	Motif	141 – 143	3	Cell attachment site Potential
	Motif	504 – 506	3	Cell attachment site Potential
	Motif	942 – 944	3	Cell attachment site Potential
	Motif	1065 – 1067	3	Cell attachment site Potential
	Motif	1068 – 1070	3	Cell attachment site Potential
	Motif	1125 – 1127	3	Cell attachment site Potential
	Motif	1134 – 1136	3	Cell attachment site Potential
Sites
	Metal binding	1312	1	Calcium By similarity
	Metal binding	1314	1	Calcium By similarity
	Metal binding	1315	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	1320	1	Calcium By similarity
Amino acid modifications
	Modified residue	288	1	4-hydroxyproline By similarity UniProtKB P05997
	Modified residue	291	1	4-hydroxyproline By similarity UniProtKB P05997
	Modified residue	294	1	4-hydroxyproline By similarity UniProtKB P05997
	Modified residue	609	1	4-hydroxyproline By similarity UniProtKB P05997
	Modified residue	615	1	4-hydroxyproline By similarity UniProtKB P05997
	Glycosylation	1260	1	N-linked (GlcNAc...) Potential
	Glycosylation	1398	1	N-linked (GlcNAc...) Potential
	Disulfide bond	1294 ↔ 1326		By similarity
	Disulfide bond	1334 ↔ 1495		By similarity
	Disulfide bond	1403 ↔ 1448		By similarity
Experimental info
	Sequence conflict	20	1	Y → D in BAE23896. Ref.2
	Sequence conflict	88	1	T → P in AAA37440. Ref.1
	Sequence conflict	160	1	G → R in BAE27850. Ref.2
	Sequence conflict	164	1	V → M in AAA37440. Ref.1
	Sequence conflict	222	1	Q → V in AAA37440. Ref.1
	Sequence conflict	231	1	V → A in AAA37440. Ref.1
	Sequence conflict	387	1	A → R in AAA37440. Ref.1
	Sequence conflict	390	1	T → H in AAA37440. Ref.1
	Sequence conflict	428	1	A → R in AAA37440. Ref.1
	Sequence conflict	431	1	P → A in AAA37440. Ref.1
	Sequence conflict	614	1	L → V in AAA37440. Ref.1
	Sequence conflict	614	1	L → V in AAH55077. Ref.3
	Sequence conflict	666	1	Q → A in AAA37440. Ref.1
	Sequence conflict	809 – 813	5	PTGEK → LLGAP in AAA37440. Ref.1
	Sequence conflict	851	1	P → S in AAA37440. Ref.1
	Sequence conflict	1001 – 1002	2	ER → VT in AAA37440. Ref.1
	Sequence conflict	1013	1	T → A in AAH55077. Ref.3
	Sequence conflict	1063	1	G → V in BAE21154. Ref.2
	Sequence conflict	1181	1	P → S in AAA37440. Ref.1
	Sequence conflict	1337	1	A → T in AAH55077. Ref.3
	Sequence conflict	1388	1	L → F in AAA37440. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q3U962 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: CAAE15514984DB41	FASTA	1,497	145,018
	10 20 30 40 50 60 MMANWVGARP LLILSVLLGY CVSIKAQEQE NDEYDEEIAC TQHGQMYLNR DIWKPSPCQI 70 80 90 100 110 120 CVCDNGAILC DKIECPEVLN CANPITPTGE CCPVCPQTGG GDTSFGRGRK GQKGEPGLVP 130 140 150 160 170 180 VVTGIRGRPG PAGPPGSQGP RGDRGPKGRP GPRGPQGIDG EPGVPGQPGA PGPPGHPSHP 190 200 210 220 230 240 GPDGMSRPFS AQMAGLDEKS GLGSQVGLMP GSVGPVGPRG PQGLQGQQGG VGPAGPPGEP 250 260 270 280 290 300 GEPGPMGPIG SRGPEGPPGK PGEDGEPGRN GNTGEVGFSG SPGARGFPGA PGLPGLKGHR 310 320 330 340 350 360 GHKGLEGPKG EIGAPGAKGE AGPTGPMGAM GPLGPRGMPG ERGRLGPQGA PGKRGAHGMP 370 380 390 400 410 420 GKPGPMGPLG IPGSSGFPGN PGMKGEAGPT GARGPEGPQG QRGETGPPGP AGSQGLPGAV 430 440 450 460 470 480 GTDGTPGAKG PTGSAGTSGP PGLAGPPGSP GPQGSTGPQG IRGQSGDPGV PGFKGEAGPK 490 500 510 520 530 540 GEPGPHGIQG PIGPPGEEGK RGPRGDPGTV GPPGPMGERG APGNRGFPGS DGLPGPKGAQ 550 560 570 580 590 600 GERGPVGSSG PKGGQGDPGR PGEPGLPGAR GLTGNPGVQG PEGKLGPLGA PGEDGRPGPP 610 620 630 640 650 660 GSIGIRGQPG SMGLPGPKGS SGDLGKPGEA GNAGVPGQRG APGKDGEVGP SGPVGPPGLA 670 680 690 700 710 720 GERGEQGPPG PTGFQGLPGP PGPPGEGGKA GDQGVPGEPG AVGPLGPRGE RGNPGERGEP 730 740 750 760 770 780 GITGLPGEKG MAGGHGPDGP KGNPGPTGTI GDTGPPGLQG MPGERGIAGT PGPKGDRGGI 790 800 810 820 830 840 GEKGAEGTAG NDGARGLPGP LGPPGPAGPT GEKGEPGPRG LVGPPGSRGN PGSRGENGPT 850 860 870 880 890 900 GAVGFAGPQG PDGQPGVKGE PGEPGQKGDA GSPGPQGLAG SPGPHGPHGV PGLKGGRGTQ 910 920 930 940 950 960 GPPGATGFPG SAGRVGPPGP AGAPGPAGPA GEPGKEGPPG LRGDPGSHGR VGDRGPAGPP 970 980 990 1000 1010 1020 GSPGDKGDPG EDGQPGPDGP PGPAGTTGQR GIVGMPGQRG ERGMPGLPGP AGTPGKVGPT 1030 1040 1050 1060 1070 1080 GATGDKGPPG PVGPPGSNGP VGEPGPEGPA GNDGTPGRDG AVGERGDRGD PGPAGLPGSQ 1090 1100 1110 1120 1130 1140 GAPGTPGPVG APGDAGQRGE PGSRGPVGPP GRAGKRGLPG PQGPRGDKGD NGDRGDRGQK 1150 1160 1170 1180 1190 1200 GHRGFTGLQG LPGPPGPNGE QGSAGIPGPF GPRGPPGPVG PSGKEGNPGP LGPIGPPGVR 1210 1220 1230 1240 1250 1260 GSVGEAGPEG PPGEPGPPGP PGPPGHLTAA LGDIMGHYDE NMPDPLPEFT EDQAAPDDTN 1270 1280 1290 1300 1310 1320 KTDPGIHVTL KSLSSQIETM RSPDGSKKHP ARTCDDLKLC HPTKQSGEYW IDPNQGSAED 1330 1340 1350 1360 1370 1380 AIKVYCNMET GETCISANPA SVPRKTWWAS KSPDNKPVWY GLDMNRGSQF TYGDYQSPNT 1390 1400 1410 1420 1430 1440 AITQMTFLRL LSKEASQNLT YICRNTVGYM DDQAKNLKKA VVLKGSNDLE IKGEGNIRFR 1450 1460 1470 1480 1490 YTVLQDTCSK RNGNVGKTIF EYRTQNVARL PIIDVGPVDI GNADQEFGLD IGPVCFM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Localization of pro-alpha 2(V) collagen transcripts in the tissues of the developing mouse embryo." Andrikopoulos K., Suzuki H.R., Solursh M., Ramirez F. Dev. Dyn. 195:113-120(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE. Strain: BALB/c.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow, Cerebellum, Embryo, Placenta and Skin.
[3]	"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]. Strain: C3H/He. Tissue: Mammary gland and Mesenchymal stem cell.
[4]	"Targeted mutation in the col5a2 gene reveals a regulatory role for type V collagen during matrix assembly." Andrikopoulos K., Liu X., Keene D.R., Jaenisch R., Ramirez F. Nat. Genet. 9:31-36(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Effect of targeted mutation in collagen V alpha 2 gene on development of cutaneous hyperplasia in tight skin mice." Phelps R.G., Murai C., Saito S., Hatakeyama A., Andrikopoulos K., Kasturi K.N., Bona C.A. Mol. Med. 4:356-360(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Development of a functional skin matrix requires deposition of collagen V heterotrimers." Chanut-Delalande H., Bonod-Bidaud C., Cogne S., Malbouyres M., Ramirez F., Fichard A., Ruggiero F. Mol. Cell. Biol. 24:6049-6057(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L02918 mRNA. Translation: AAA37440.1. AK132413 mRNA. Translation: BAE21154.1. AK139130 mRNA. Translation: BAE23896.1. Different initiation. AK147220 mRNA. Translation: BAE27775.1. AK147328 mRNA. Translation: BAE27850.1. AK151929 mRNA. Translation: BAE30805.1. AK160008 mRNA. Translation: BAE35556.1. BC043696 mRNA. Translation: AAH43696.1. BC055077 mRNA. Translation: AAH55077.1.
IPI	IPI00121120.
PIR	I49607.
RefSeq	NP_031763.2. NM_007737.2.
UniGene	Mm.10299.
3D structure databases
ProteinModelPortal	Q3U962.
SMR	Q3U962. Positions 1282-1497.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000083620.
PTM databases
PhosphoSite	Q3U962.
Proteomic databases
PaxDb	Q3U962.
PRIDE	Q3U962.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000086430; ENSMUSP00000083620; ENSMUSG00000026042.
GeneID	12832.
KEGG	mmu:12832.
UCSC	uc007awr.1. mouse.
Organism-specific databases
CTD	1290.
MGI	MGI:88458. Col5a2.
Phylogenomic databases
eggNOG	NOG12793.
GeneTree	ENSGT00660000095287.
HOVERGEN	HBG004933.
InParanoid	Q3U962.
KO	K06236.
OMA	PDHKPVW.
OrthoDB	EOG4K0QMS.
Gene expression databases
Bgee	Q3U962.
CleanEx	MM_COL5A2.
Genevestigator	Q3U962.
Family and domain databases
InterPro	IPR008160. Collagen. IPR000885. Fib_collagen_C. IPR001007. VWF_C. [Graphical view]
Pfam	PF01410. COLFI. 1 hit. PF01391. Collagen. 7 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. mouse.
NextBio	282338.
SOURCE	Search...

Entry information

Entry name

CO5A2_MOUSE

Accession

Primary (citable) accession number: Q3U962
Secondary accession number(s): Q3TVR2 , Q3UHK7, Q3UTT4, Q3V1J6, Q61431, Q7TMS0, Q80VS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	October 11, 2005
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program