ID   B1AWB9_MOUSE            Unreviewed;      1838 AA.
AC   B1AWB9;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   SubName: Full=Collagen, type V, alpha 1 {ECO:0000313|EMBL:AAI38448.1};
GN   Name=Col5a1 {ECO:0000313|EMBL:AAI38448.1, ECO:0000313|MGI:MGI:88457};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAI38448.1};
RN   [1] {ECO:0000313|EMBL:AAI38448.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000313|EMBL:AAI38448.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   EMBL; BC138447; AAI38448.1; -; mRNA.
DR   EMBL; BC138449; AAI38450.1; -; mRNA.
DR   RefSeq; NP_056549.2; NM_015734.2.
DR   SMR; B1AWB9; -.
DR   PeptideAtlas; B1AWB9; -.
DR   Antibodypedia; 3446; 491 antibodies from 37 providers.
DR   DNASU; 12831; -.
DR   GeneID; 12831; -.
DR   KEGG; mmu:12831; -.
DR   AGR; MGI:88457; -.
DR   CTD; 1289; -.
DR   MGI; MGI:88457; Col5a1.
DR   VEuPathDB; HostDB:ENSMUSG00000026837; -.
DR   HOGENOM; CLU_001074_2_1_1; -.
DR   OMA; TQGFQGK; -.
DR   OrthoDB; 2970887at2759; -.
DR   BioGRID-ORCS; 12831; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Col5a1; mouse.
DR   ExpressionAtlas; B1AWB9; baseline and differential.
DR   GO; GO:0005588; C:collagen type V trimer; IEA:Ensembl.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR   GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl.
DR   GO; GO:0043394; F:proteoglycan binding; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
DR   GO; GO:0032964; P:collagen biosynthetic process; IEA:Ensembl.
DR   GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR   GO; GO:0048592; P:eye morphogenesis; IEA:Ensembl.
DR   GO; GO:0045112; P:integrin biosynthetic process; IEA:Ensembl.
DR   GO; GO:1903225; P:negative regulation of endodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0043588; P:skin development; IEA:Ensembl.
DR   GO; GO:0035313; P:wound healing, spreading of epidermal cells; IEA:Ensembl.
DR   CDD; cd00110; LamG; 1.
DR   Gene3D; 2.60.120.1000; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000885; Fib_collagen_C.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR048287; TSPN-like_N.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF387; COLLAGEN ALPHA-1(V) CHAIN; 1.
DR   Pfam; PF01410; COLFI; 1.
DR   Pfam; PF01391; Collagen; 6.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   SMART; SM00038; COLFI; 1.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51461; NC1_FIB; 1.
PE   1: Evidence at protein level;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:AAI38448.1};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..1838
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015087029"
FT   DOMAIN          1609..1837
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000259|PROSITE:PS51461"
FT   REGION          242..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..1574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..409
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..483
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..700
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..816
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        946..973
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1156..1170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1321..1357
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1381..1396
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1454..1468
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1525..1540
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1559..1573
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1838 AA;  183677 MW;  D20F4E5198A09ECF CRC64;
     MDVHTRWKAA RPGALLLSSP LLLFLLLLWA PPSSRAAQPA DLLEMLDFHN LPSGVTKTTG
     FCATRRSSSE PDVAYRVSKD AQLSMPTKQL YPESGFPEDF SILTTVKAKK GSQAFLVSIY
     NEQGIQQLGL ELGRSPVFLY EDHTGKPGPE EYPLFPGINL SDGKWHRIAL SVYKKNVTLI
     LDCKKKITKF LSRSDHPIID TNGIVMFGSR ILDDEIFEGD IQQLLFVSDN RAAYDYCEHY
     SPDCDTAVPD TPQSQDPNPD EYYPEGEGET YYYEYPYYED PEDPGKEPAP TQKPVEAARE
     TTEVPEEQTQ PLPEAPTVPE TSDTADKEDS LGIGDYDYVP PDDYYTPPPY EDFGYGEGVE
     NPDQPTNPDS GAEVPTSTTV TSNTSNPAPG EGKDDLGGEF TEETIKNLEE NYYDPYFDPD
     SDSSVSPSEI GPGMPANQDT IFEGIGGPRG EKGQKGEPAI IEPGMLIEGP PGPEGPAGLP
     GPPGTTGPTG QMGDPGERGP PGRPGLPGAD GLPGPPGTML MLPFRFGGGG DAGSKGPMVS
     AQESQAQAIL QQARLALRGP AGPMGLTGRP GPMGPPGSGG LKGEPGDMGP QGPRGVQGPP
     GPTGKPGRRG RAGSDGARGM PGQTGPKGDR GFDGLAGLPG EKGHRGDPGP SGPPGIPGDD
     GERGDDGEVG PRGLPGEPGP RGLLGPKGPP GPPGPPGVTG MDGQPGPKGN VGPQGEPGPP
     GQQGNPGAQG LPGPQGAIGP PGEKGPLGKP GLPGMPGADG PPGHPGKEGP PGEKGGQGPP
     GPQGPIGYPG PRGVKGADGI RGLKGTKGEK GEDGFPGFKG DMGIKGDRGE IGPPGPRGED
     GPEGPKGRGG PNGDPGPLGP TGEKGKLGVP GLPGYPGRQG PKGSIGFPGF PGANGEKGGR
     GTPGKPGPRG QRGPTGPRGE RGPRGITGKP GPKGNSGGDG PAGPPGERGP NGPQGPTGFP
     GPKGPPGPPG KDGLPGHPGQ RGETGFQGKT GPPGPPGVVG PQGPTGETGP MGERGHPGPP
     GPPGEQGLPG AAGKEGTKGD PGPAGLPGKD GPPGLRGFPG DRGLPGPVGA LGLKGSEGPP
     GPPGPAGSPG ERGPAGAAGP IGIPGRPGPQ GPPGPAGEKG LPGEKGPQGP AGRDGLQGPV
     GLPGPAGPVG PPGEDGDKGE IGEPGQKGSK GDKGEQGPPG PTGPQGPIGQ PGPSGADGEP
     GPRGQQGLFG QKGDEGSRGF PGPPGPVGLQ GLPGPPGEKG ETGDVGQMGP PGPPGPRGPS
     GAPGADGPQG PPGGIGNPGA VGEKGEPGEA GDPGLPGEGG PLGPKGERGE KGEAGPSGAA
     GPPGPKGPPG DDGPKGSPGP VGFPGDPGPP GEPGPAGQDG PPGDKGDDGE PGQTGSPGPT
     GEPGPSGPPG KRGPPGPAGP EGRQGEKGAK GEAGLEGPPG KTGPIGPQGA PGKPGPDGLR
     GIPGPVGEQG LPGSPGPDGP PGPMGPPGLP GLKGDSGPKG EKGHPGLIGL IGPPGEQGEK
     GDRGLPGPQG SSGPKGDQGI TGPSGPLGPP GPPGLPGPPG PKGAKGSSGP TGPKGEAGHP
     GLPGPPGPPG EVIQPLPIQA SRTRRNIDAS QLLDDGAGES YVDYADGMEE IFGSLNSLKL
     EIEQMKRPLG TQQNPARTCK DLQLCHPDFP DGEYWVDPNQ GCSRDSFKVY CNFTAGGSTC
     VFPDKKSEGA RITSWPKENP GSWFSEFKRG KLLSYVDAEG NPVGVVQMTF LRLLSASAHQ
     NVTYNCYQSV AWQDAATGSY DKAIRFLGSN DEEMSYDNNP YIRALVDGCA TKKGYQKTVL
     EIDTPKVEQV PIVDIMFNDF GEASQKFGFE VGPACFLG
//