SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q3U962

- CO5A2_MOUSE

UniProt

Q3U962 - CO5A2_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 – 13121Calcium By similarity
Metal bindingi1314 – 13141Calcium By similarity
Metal bindingi1315 – 13151Calcium; via carbonyl oxygen By similarity
Metal bindingi1320 – 13201Calcium By 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:Col5a2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:88458. Col5a2.

Subcellular locationi

GO - Cellular componenti

  1. collagen trimer Source: MGI
  2. collagen type V trimer Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626 Reviewed predictionAdd
BLAST
Chaini27 – 12271201Collagen alpha-2(V) chainPRO_0000283768Add
BLAST
Propeptidei1228 – 1497270C-terminal propeptidePRO_0000283769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei288 – 28814-hydroxyproline By similarityBy similarity
Modified residuei291 – 29114-hydroxyproline By similarityBy similarity
Modified residuei294 – 29414-hydroxyproline By similarityBy similarity
Modified residuei609 – 60914-hydroxyproline By similarityBy similarity
Modified residuei615 – 61514-hydroxyproline By similarityBy similarity
Glycosylationi1260 – 12601N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1294 ↔ 1326 By similarity
Disulfide bondi1334 ↔ 1495 By similarity
Glycosylationi1398 – 13981N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1403 ↔ 1448 By similarity

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.By similarity
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

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 1282-1497.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 9659VWFCAdd
BLAST
Domaini1264 – 1497234Fibrillar collagen NC1Add
BLAST

Motif

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

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.

Sequence similaritiesi

Contains 1 VWFC domain.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00740000114967.
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

MMANWVGARP LLILSVLLGY CVSIKAQEQE NDEYDEEIAC TQHGQMYLNR     50
DIWKPSPCQI CVCDNGAILC DKIECPEVLN CANPITPTGE CCPVCPQTGG 100
GDTSFGRGRK GQKGEPGLVP VVTGIRGRPG PAGPPGSQGP RGDRGPKGRP 150
GPRGPQGIDG EPGVPGQPGA PGPPGHPSHP GPDGMSRPFS AQMAGLDEKS 200
GLGSQVGLMP GSVGPVGPRG PQGLQGQQGG VGPAGPPGEP GEPGPMGPIG 250
SRGPEGPPGK PGEDGEPGRN GNTGEVGFSG SPGARGFPGA PGLPGLKGHR 300
GHKGLEGPKG EIGAPGAKGE AGPTGPMGAM GPLGPRGMPG ERGRLGPQGA 350
PGKRGAHGMP GKPGPMGPLG IPGSSGFPGN PGMKGEAGPT GARGPEGPQG 400
QRGETGPPGP AGSQGLPGAV GTDGTPGAKG PTGSAGTSGP PGLAGPPGSP 450
GPQGSTGPQG IRGQSGDPGV PGFKGEAGPK GEPGPHGIQG PIGPPGEEGK 500
RGPRGDPGTV GPPGPMGERG APGNRGFPGS DGLPGPKGAQ GERGPVGSSG 550
PKGGQGDPGR PGEPGLPGAR GLTGNPGVQG PEGKLGPLGA PGEDGRPGPP 600
GSIGIRGQPG SMGLPGPKGS SGDLGKPGEA GNAGVPGQRG APGKDGEVGP 650
SGPVGPPGLA GERGEQGPPG PTGFQGLPGP PGPPGEGGKA GDQGVPGEPG 700
AVGPLGPRGE RGNPGERGEP GITGLPGEKG MAGGHGPDGP KGNPGPTGTI 750
GDTGPPGLQG MPGERGIAGT PGPKGDRGGI GEKGAEGTAG NDGARGLPGP 800
LGPPGPAGPT GEKGEPGPRG LVGPPGSRGN PGSRGENGPT GAVGFAGPQG 850
PDGQPGVKGE PGEPGQKGDA GSPGPQGLAG SPGPHGPHGV PGLKGGRGTQ 900
GPPGATGFPG SAGRVGPPGP AGAPGPAGPA GEPGKEGPPG LRGDPGSHGR 950
VGDRGPAGPP GSPGDKGDPG EDGQPGPDGP PGPAGTTGQR GIVGMPGQRG 1000
ERGMPGLPGP AGTPGKVGPT GATGDKGPPG PVGPPGSNGP VGEPGPEGPA 1050
GNDGTPGRDG AVGERGDRGD PGPAGLPGSQ GAPGTPGPVG APGDAGQRGE 1100
PGSRGPVGPP GRAGKRGLPG PQGPRGDKGD NGDRGDRGQK GHRGFTGLQG 1150
LPGPPGPNGE QGSAGIPGPF GPRGPPGPVG PSGKEGNPGP LGPIGPPGVR 1200
GSVGEAGPEG PPGEPGPPGP PGPPGHLTAA LGDIMGHYDE NMPDPLPEFT 1250
EDQAAPDDTN KTDPGIHVTL KSLSSQIETM RSPDGSKKHP ARTCDDLKLC 1300
HPTKQSGEYW IDPNQGSAED AIKVYCNMET GETCISANPA SVPRKTWWAS 1350
KSPDNKPVWY GLDMNRGSQF TYGDYQSPNT AITQMTFLRL LSKEASQNLT 1400
YICRNTVGYM DDQAKNLKKA VVLKGSNDLE IKGEGNIRFR YTVLQDTCSK 1450
RNGNVGKTIF EYRTQNVARL PIIDVGPVDI GNADQEFGLD IGPVCFM 1497
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201Y → D in BAE23896. 1 Publication
Sequence conflicti88 – 881T → P in AAA37440. 1 Publication
Sequence conflicti160 – 1601G → R in BAE27850. 1 Publication
Sequence conflicti164 – 1641V → M in AAA37440. 1 Publication
Sequence conflicti222 – 2221Q → V in AAA37440. 1 Publication
Sequence conflicti231 – 2311V → A in AAA37440. 1 Publication
Sequence conflicti387 – 3871A → R in AAA37440. 1 Publication
Sequence conflicti390 – 3901T → H in AAA37440. 1 Publication
Sequence conflicti428 – 4281A → R in AAA37440. 1 Publication
Sequence conflicti431 – 4311P → A in AAA37440. 1 Publication
Sequence conflicti614 – 6141L → V in AAA37440. 1 Publication
Sequence conflicti614 – 6141L → V in AAH55077. 1 Publication
Sequence conflicti666 – 6661Q → A in AAA37440. 1 Publication
Sequence conflicti809 – 8135PTGEK → LLGAP in AAA37440. 1 Publication
Sequence conflicti851 – 8511P → S in AAA37440. 1 Publication
Sequence conflicti1001 – 10022ER → VT in AAA37440. 1 Publication
Sequence conflicti1013 – 10131T → A in AAH55077. 1 Publication
Sequence conflicti1063 – 10631G → V in BAE21154. 1 Publication
Sequence conflicti1181 – 11811P → S in AAA37440. 1 Publication
Sequence conflicti1337 – 13371A → T in AAH55077. 1 Publication
Sequence conflicti1388 – 13881L → F in AAA37440. 1 Publication

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 1282-1497.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000083620.

PTM databases

PhosphoSitei Q3U962.

Proteomic databases

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 ENSGT00740000114967.
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/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.

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: September 3, 2014
This is version 71 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

Similar proteinsi