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Q3U962 (CO5A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-2(V) chain
Gene names
Name:Col5a2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1497 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secretedextracellular spaceextracellular 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 12271201Collagen alpha-2(V) chain
PRO_0000283768
Propeptide1228 – 1497270C-terminal propeptide
PRO_0000283769

Regions

Domain38 – 9659VWFC
Domain1264 – 1497234Fibrillar collagen NC1
Motif141 – 1433Cell attachment site Potential
Motif504 – 5063Cell attachment site Potential
Motif942 – 9443Cell attachment site Potential
Motif1065 – 10673Cell attachment site Potential
Motif1068 – 10703Cell attachment site Potential
Motif1125 – 11273Cell attachment site Potential
Motif1134 – 11363Cell attachment site Potential

Sites

Metal binding13121Calcium By similarity
Metal binding13141Calcium By similarity
Metal binding13151Calcium; via carbonyl oxygen By similarity
Metal binding13201Calcium By similarity

Amino acid modifications

Modified residue28814-hydroxyproline By similarity UniProtKB P05997
Modified residue29114-hydroxyproline By similarity UniProtKB P05997
Modified residue29414-hydroxyproline By similarity UniProtKB P05997
Modified residue60914-hydroxyproline By similarity UniProtKB P05997
Modified residue61514-hydroxyproline By similarity UniProtKB P05997
Glycosylation12601N-linked (GlcNAc...) Potential
Glycosylation13981N-linked (GlcNAc...) Potential
Disulfide bond1294 ↔ 1326 By similarity
Disulfide bond1334 ↔ 1495 By similarity
Disulfide bond1403 ↔ 1448 By similarity

Experimental info

Sequence conflict201Y → D in BAE23896. Ref.2
Sequence conflict881T → P in AAA37440. Ref.1
Sequence conflict1601G → R in BAE27850. Ref.2
Sequence conflict1641V → M in AAA37440. Ref.1
Sequence conflict2221Q → V in AAA37440. Ref.1
Sequence conflict2311V → A in AAA37440. Ref.1
Sequence conflict3871A → R in AAA37440. Ref.1
Sequence conflict3901T → H in AAA37440. Ref.1
Sequence conflict4281A → R in AAA37440. Ref.1
Sequence conflict4311P → A in AAA37440. Ref.1
Sequence conflict6141L → V in AAA37440. Ref.1
Sequence conflict6141L → V in AAH55077. Ref.3
Sequence conflict6661Q → A in AAA37440. Ref.1
Sequence conflict809 – 8135PTGEK → LLGAP in AAA37440. Ref.1
Sequence conflict8511P → S in AAA37440. Ref.1
Sequence conflict1001 – 10022ER → VT in AAA37440. Ref.1
Sequence conflict10131T → A in AAH55077. Ref.3
Sequence conflict10631G → V in BAE21154. Ref.2
Sequence conflict11811P → S in AAA37440. Ref.1
Sequence conflict13371A → T in AAH55077. Ref.3
Sequence conflict13881L → F in AAA37440. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3U962 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: CAAE15514984DB41

FASTA1,497145,018
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
PIRI49607.
RefSeqNP_031763.2. NM_007737.2.
UniGeneMm.10299.

3D structure databases

ProteinModelPortalQ3U962.
SMRQ3U962. Positions 33-101, 1282-1497.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000083620.

PTM databases

PhosphoSiteQ3U962.

Proteomic databases

PaxDbQ3U962.
PRIDEQ3U962.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000086430; ENSMUSP00000083620; ENSMUSG00000026042.
GeneID12832.
KEGGmmu:12832.
UCSCuc007awr.1. mouse.

Organism-specific databases

CTD1290.
MGIMGI:88458. Col5a2.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00740000114967.
HOVERGENHBG004933.
InParanoidQ3U962.
KOK06236.
OMAPDHKPVW.
OrthoDBEOG7TJ3HH.
PhylomeDBQ3U962.
TreeFamTF344135.

Gene expression databases

BgeeQ3U962.
CleanExMM_COL5A2.
GenevestigatorQ3U962.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 7 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL5A2. mouse.
NextBio282338.
PROQ3U962.
SOURCESearch...

Entry information

Entry nameCO5A2_MOUSE
AccessionPrimary (citable) accession number: Q3U962
Secondary accession number(s): Q3TVR2 expand/collapse secondary AC list , Q3UHK7, Q3UTT4, Q3V1J6, Q61431, Q7TMS0, Q80VS8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 11, 2005
Last modified: April 16, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot