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Q3U962

- CO5A2_MOUSE

UniProt

Q3U962 - CO5A2_MOUSE

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Protein

Collagen alpha-2(V) chain

Gene

Col5a2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1312 – 13121CalciumBy similarity
Metal bindingi1314 – 13141CalciumBy similarity
Metal bindingi1315 – 13151Calcium; via carbonyl oxygenBy similarity
Metal bindingi1320 – 13201CalciumBy similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: InterPro
  2. metal ion binding Source: UniProtKB-KW
  3. SMAD binding Source: MGI

GO - Biological processi

  1. cellular response to amino acid stimulus Source: MGI
  2. collagen fibril organization Source: UniProtKB
  3. eye morphogenesis Source: Ensembl
  4. skeletal system development Source: MGI
  5. skin development Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_196644. Syndecan interactions.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-2(V) chain
Gene namesi
Name:Col5a2Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:88458. Col5a2.

Subcellular locationi

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

GO - Cellular componenti

  1. collagen trimer Source: MGI
  2. collagen type V trimer Source: Ensembl
  3. extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 12271201Collagen alpha-2(V) chainSequence AnalysisPRO_0000283768Add
BLAST
Propeptidei1228 – 1497270C-terminal propeptideSequence AnalysisPRO_0000283769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei288 – 28814-hydroxyprolineBy similarity
Modified residuei291 – 29114-hydroxyprolineBy similarity
Modified residuei294 – 29414-hydroxyprolineBy similarity
Modified residuei609 – 60914-hydroxyprolineBy similarity
Modified residuei615 – 61514-hydroxyprolineBy similarity
Glycosylationi1260 – 12601N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1294 ↔ 1326PROSITE-ProRule annotation
Disulfide bondi1334 ↔ 1495PROSITE-ProRule annotation
Glycosylationi1398 – 13981N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1403 ↔ 1448PROSITE-ProRule annotation

Post-translational modificationi

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.
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

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiQ3U962.
PaxDbiQ3U962.
PRIDEiQ3U962.

PTM databases

PhosphoSiteiQ3U962.

Expressioni

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ3U962.
CleanExiMM_COL5A2.
GenevestigatoriQ3U962.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000083620.

Structurei

3D structure databases

ProteinModelPortaliQ3U962.
SMRiQ3U962. Positions 36-76, 1282-1497.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 9659VWFCPROSITE-ProRule annotationAdd
BLAST
Domaini1264 – 1497234Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi141 – 1433Cell attachment siteSequence Analysis
Motifi504 – 5063Cell attachment siteSequence Analysis
Motifi942 – 9443Cell attachment siteSequence Analysis
Motifi1065 – 10673Cell attachment siteSequence Analysis
Motifi1068 – 10703Cell attachment siteSequence Analysis
Motifi1125 – 11273Cell attachment siteSequence Analysis
Motifi1134 – 11363Cell attachment siteSequence Analysis

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000118776.
HOVERGENiHBG004933.
InParanoidiQ3U962.
KOiK06236.
OMAiIGIRGQP.
OrthoDBiEOG7TJ3HH.
PhylomeDBiQ3U962.
TreeFamiTF344135.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 7 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3U962-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMANWVGARP LLILSVLLGY CVSIKAQEQE NDEYDEEIAC TQHGQMYLNR
60 70 80 90 100
DIWKPSPCQI CVCDNGAILC DKIECPEVLN CANPITPTGE CCPVCPQTGG
110 120 130 140 150
GDTSFGRGRK GQKGEPGLVP VVTGIRGRPG PAGPPGSQGP RGDRGPKGRP
160 170 180 190 200
GPRGPQGIDG EPGVPGQPGA PGPPGHPSHP GPDGMSRPFS AQMAGLDEKS
210 220 230 240 250
GLGSQVGLMP GSVGPVGPRG PQGLQGQQGG VGPAGPPGEP GEPGPMGPIG
260 270 280 290 300
SRGPEGPPGK PGEDGEPGRN GNTGEVGFSG SPGARGFPGA PGLPGLKGHR
310 320 330 340 350
GHKGLEGPKG EIGAPGAKGE AGPTGPMGAM GPLGPRGMPG ERGRLGPQGA
360 370 380 390 400
PGKRGAHGMP GKPGPMGPLG IPGSSGFPGN PGMKGEAGPT GARGPEGPQG
410 420 430 440 450
QRGETGPPGP AGSQGLPGAV GTDGTPGAKG PTGSAGTSGP PGLAGPPGSP
460 470 480 490 500
GPQGSTGPQG IRGQSGDPGV PGFKGEAGPK GEPGPHGIQG PIGPPGEEGK
510 520 530 540 550
RGPRGDPGTV GPPGPMGERG APGNRGFPGS DGLPGPKGAQ GERGPVGSSG
560 570 580 590 600
PKGGQGDPGR PGEPGLPGAR GLTGNPGVQG PEGKLGPLGA PGEDGRPGPP
610 620 630 640 650
GSIGIRGQPG SMGLPGPKGS SGDLGKPGEA GNAGVPGQRG APGKDGEVGP
660 670 680 690 700
SGPVGPPGLA GERGEQGPPG PTGFQGLPGP PGPPGEGGKA GDQGVPGEPG
710 720 730 740 750
AVGPLGPRGE RGNPGERGEP GITGLPGEKG MAGGHGPDGP KGNPGPTGTI
760 770 780 790 800
GDTGPPGLQG MPGERGIAGT PGPKGDRGGI GEKGAEGTAG NDGARGLPGP
810 820 830 840 850
LGPPGPAGPT GEKGEPGPRG LVGPPGSRGN PGSRGENGPT GAVGFAGPQG
860 870 880 890 900
PDGQPGVKGE PGEPGQKGDA GSPGPQGLAG SPGPHGPHGV PGLKGGRGTQ
910 920 930 940 950
GPPGATGFPG SAGRVGPPGP AGAPGPAGPA GEPGKEGPPG LRGDPGSHGR
960 970 980 990 1000
VGDRGPAGPP GSPGDKGDPG EDGQPGPDGP PGPAGTTGQR GIVGMPGQRG
1010 1020 1030 1040 1050
ERGMPGLPGP AGTPGKVGPT GATGDKGPPG PVGPPGSNGP VGEPGPEGPA
1060 1070 1080 1090 1100
GNDGTPGRDG AVGERGDRGD PGPAGLPGSQ GAPGTPGPVG APGDAGQRGE
1110 1120 1130 1140 1150
PGSRGPVGPP GRAGKRGLPG PQGPRGDKGD NGDRGDRGQK GHRGFTGLQG
1160 1170 1180 1190 1200
LPGPPGPNGE QGSAGIPGPF GPRGPPGPVG PSGKEGNPGP LGPIGPPGVR
1210 1220 1230 1240 1250
GSVGEAGPEG PPGEPGPPGP PGPPGHLTAA LGDIMGHYDE NMPDPLPEFT
1260 1270 1280 1290 1300
EDQAAPDDTN KTDPGIHVTL KSLSSQIETM RSPDGSKKHP ARTCDDLKLC
1310 1320 1330 1340 1350
HPTKQSGEYW IDPNQGSAED AIKVYCNMET GETCISANPA SVPRKTWWAS
1360 1370 1380 1390 1400
KSPDNKPVWY GLDMNRGSQF TYGDYQSPNT AITQMTFLRL LSKEASQNLT
1410 1420 1430 1440 1450
YICRNTVGYM DDQAKNLKKA VVLKGSNDLE IKGEGNIRFR YTVLQDTCSK
1460 1470 1480 1490
RNGNVGKTIF EYRTQNVARL PIIDVGPVDI GNADQEFGLD IGPVCFM
Length:1,497
Mass (Da):145,018
Last modified:October 11, 2005 - v1
Checksum:iCAAE15514984DB41
GO

Sequence cautioni

The sequence BAE23896.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201Y → D in BAE23896. (PubMed:16141072)Curated
Sequence conflicti88 – 881T → P in AAA37440. (PubMed:1297453)Curated
Sequence conflicti160 – 1601G → R in BAE27850. (PubMed:16141072)Curated
Sequence conflicti164 – 1641V → M in AAA37440. (PubMed:1297453)Curated
Sequence conflicti222 – 2221Q → V in AAA37440. (PubMed:1297453)Curated
Sequence conflicti231 – 2311V → A in AAA37440. (PubMed:1297453)Curated
Sequence conflicti387 – 3871A → R in AAA37440. (PubMed:1297453)Curated
Sequence conflicti390 – 3901T → H in AAA37440. (PubMed:1297453)Curated
Sequence conflicti428 – 4281A → R in AAA37440. (PubMed:1297453)Curated
Sequence conflicti431 – 4311P → A in AAA37440. (PubMed:1297453)Curated
Sequence conflicti614 – 6141L → V in AAA37440. (PubMed:1297453)Curated
Sequence conflicti614 – 6141L → V in AAH55077. (PubMed:15489334)Curated
Sequence conflicti666 – 6661Q → A in AAA37440. (PubMed:1297453)Curated
Sequence conflicti809 – 8135PTGEK → LLGAP in AAA37440. (PubMed:1297453)Curated
Sequence conflicti851 – 8511P → S in AAA37440. (PubMed:1297453)Curated
Sequence conflicti1001 – 10022ER → VT in AAA37440. (PubMed:1297453)Curated
Sequence conflicti1013 – 10131T → A in AAH55077. (PubMed:15489334)Curated
Sequence conflicti1063 – 10631G → V in BAE21154. (PubMed:16141072)Curated
Sequence conflicti1181 – 11811P → S in AAA37440. (PubMed:1297453)Curated
Sequence conflicti1337 – 13371A → T in AAH55077. (PubMed:15489334)Curated
Sequence conflicti1388 – 13881L → F in AAA37440. (PubMed:1297453)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS35555.1.
PIRiI49607.
RefSeqiNP_031763.2. NM_007737.2.
UniGeneiMm.10299.

Genome annotation databases

EnsembliENSMUST00000086430; ENSMUSP00000083620; ENSMUSG00000026042.
GeneIDi12832.
KEGGimmu:12832.
UCSCiuc007awr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS35555.1.
PIRi I49607.
RefSeqi NP_031763.2. NM_007737.2.
UniGenei Mm.10299.

3D structure databases

ProteinModelPortali Q3U962.
SMRi Q3U962. Positions 36-76, 1282-1497.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000083620.

PTM databases

PhosphoSitei Q3U962.

Proteomic databases

MaxQBi Q3U962.
PaxDbi Q3U962.
PRIDEi Q3U962.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000086430 ; ENSMUSP00000083620 ; ENSMUSG00000026042 .
GeneIDi 12832.
KEGGi mmu:12832.
UCSCi uc007awr.1. mouse.

Organism-specific databases

CTDi 1290.
MGIi MGI:88458. Col5a2.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118776.
HOVERGENi HBG004933.
InParanoidi Q3U962.
KOi K06236.
OMAi IGIRGQP.
OrthoDBi EOG7TJ3HH.
PhylomeDBi Q3U962.
TreeFami TF344135.

Enzyme and pathway databases

Reactomei REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_196644. Syndecan interactions.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.

Miscellaneous databases

ChiTaRSi COL5A2. mouse.
NextBioi 282338.
PROi Q3U962.
SOURCEi Search...

Gene expression databases

Bgeei Q3U962.
CleanExi MM_COL5A2.
Genevestigatori Q3U962.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 7 hits.
PF00093. VWC. 1 hit.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view ]
PROSITEi PS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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/cImported.
  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/6JImported.
    Tissue: Bone marrowImported, CerebellumImported, EmbryoImported, PlacentaImported and SkinImported.
  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/HeImported.
    Tissue: Mammary glandImported and Mesenchymal stem cellImported.
  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.

Entry informationi

Entry nameiCO5A2_MOUSE
AccessioniPrimary (citable) accession number: Q3U962
Secondary accession number(s): Q3TVR2
, Q3UHK7, Q3UTT4, Q3V1J6, Q61431, Q7TMS0, Q80VS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 11, 2005
Last modified: October 29, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.3 Publications
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.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3