ID F1LPD0_RAT Unreviewed; 1323 AA.
AC F1LPD0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Collagen type XV alpha 1 chain {ECO:0000313|Ensembl:ENSRNOP00000017217.8};
GN Name=Col15a1 {ECO:0000313|Ensembl:ENSRNOP00000017217.8,
GN ECO:0000313|RGD:1310820};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000017217.8, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000017217.8, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000017217.8,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:16641100}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000017217.8}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000017217.8};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR AlphaFoldDB; F1LPD0; -.
DR STRING; 10116.ENSRNOP00000017217; -.
DR Ensembl; ENSRNOT00000017217.8; ENSRNOP00000017217.8; ENSRNOG00000060381.2.
DR AGR; RGD:1310820; -.
DR RGD; 1310820; Col15a1.
DR VEuPathDB; HostDB:ENSRNOG00000060381; -.
DR GeneTree; ENSGT00940000158302; -.
DR HOGENOM; CLU_004003_0_0_1; -.
DR InParanoid; F1LPD0; -.
DR TreeFam; TF315821; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000039197; Expressed in skeletal muscle tissue and 7 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR CDD; cd00247; Endostatin-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF912; COLLAGEN ALPHA-1(XV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 1: Evidence at protein level;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
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..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1323
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035224242"
FT DOMAIN 40..228
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 89..227
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 269..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..696
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1323 AA; 136072 MW; 3C7003B84ECF5154 CRC64;
MTHRRTAQGR RPRWLLSIIS TLLSTVLQTR AATGSASQDH LDLTELIGVP LPSSVSFVTG
YGGFPAYSFR PGANVGRPAR TLIPSTFFRD FAIGVAVKPS SAQGGVLFAV TDAFQKVIYL
GLRLSRVEDG RQRVILYYTE PGSHVSQEAA AFSVPVMTNR WNRFAVTVQG EEAVLFMDCE
EHSQVLFQRS SRPLTFEPSA GIFVGNAGAT GLERFTGSIQ QLIIYSDPRT PEELCEAQES
SASGEASGFQ EMDEVAEIME AVTYTQAPPK EAHVDPISMP PTSSSPTEDT ELSGEPVPEG
TPGTDLSITG HSSPEQGSGE ILNDTLEVRT VDGNPSTDGG SGDGALLNVT DGQGLSATAT
GETRVPVTTA LEVENGSMPT GSPTLAMFTQ SFREVDMLDL ENLTTASGDG EVPTSTDVDT
EAGTLPTGGP TLKPREEATL GSLGEEWSTT VVSKVPLNAF EEEEASGTAI DSLDAFTPTV
VLEQASGTPT DIQAALTTTV APEQVFTAAP TDGEDLVTST EESDEEGSGS TLPIGPPLSK
PTVTPERQVT LAGVEAEGSD PVWGVDVGSG SGDIVGNEDL LRGPPGPPGP PGSPGIPGKP
GTDVFVGPPG SPGEDGAPGE PGPQGPEGQP GLDGASGQPG MKGEKGARGP NGSVGEKGDP
GSRGLPGPPG KNGEVGIPGA MGPPGPPGPP GPPGPGCTTK LGFEGPKGEK GEQGAKGERG
TDGISTMGPP GPRGPPGRVE VLSSSLINIT NGSMNFSDIP ELMGPPGPDG VPGLPGFPGP
RGPKGDTGVP GFPGLKGEQG EKGEPGAILT GDIPLEMVKG RKGEPGVHGA PGPMGPKGPP
GHKGEFGLPG RPGRPGLNGL KGAKGDRGIM LPGPPGLPGP PGPPGPPGAV VNIKGAVFPI
PARPHCKTPV GTAHPGDPEL VTFHGVKGEK GSWGLPGTKG EKGDQGAQGP PGPPVDPAYL
RHFLNSLKGE NGDAAFRGES SHNLFVSGPP GLPGHPGLAG QKGEAVVGPQ GPPGIPGLPG
PPGFGRPGVP GPPGPPGPPG PPAILGAAVP LPGPPGPPGQ PGLPGSRNLV TALSDMGDML
QKAHLVIEGT FIYLRESGEF FLRVRDGWKK LQLGELIPIP ADSPPPPALS SNPYQPQPPL
NPILSANYER PVLHLVALNT PVAGDIRADF QCFQQARAAG LLSTFRAFLS SHLQDLSTVV
RKAERFSLPI VNLKGQVLFN NWDSIFSGDG GQFNTHIPIY SFDGRDVMTD PSWPQKVVWH
GSNPHGVRLV DKYCEAWRTT DMAVTGFASP LSTGKILDQK AYSCANRLIV LCIENSFMTD
ARK
//
