ID F6Q947_HORSE Unreviewed; 1388 AA.
AC F6Q947;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 28-JAN-2026, entry version 77.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSECAP00000018945.2,
GN ECO:0000313|VGNC:VGNC:16725};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000018945.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000018945.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000018945.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000018945.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000018945.2};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSECAP00000018945.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000018945.2};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Restin potently inhibits angiogenesis.
CC {ECO:0000256|ARBA:ARBA00058706}.
CC -!- FUNCTION: Structural protein that stabilizes microvessels and muscle
CC cells, both in heart and in skeletal muscle.
CC {ECO:0000256|ARBA:ARBA00058695}.
CC -!- SUBUNIT: Interacts moderately with EFEMP2.
CC {ECO:0000256|ARBA:ARBA00065596}.
CC -!- SUBUNIT: Trimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00061770}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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DR RefSeq; XP_023485507.1; XM_023629739.2.
DR SMR; F6Q947; -.
DR FunCoup; F6Q947; 214.
DR STRING; 9796.ENSECAP00000018945; -.
DR PaxDb; 9796-ENSECAP00000018945; -.
DR Ensembl; ENSECAT00000022897.4; ENSECAP00000018945.2; ENSECAG00000021211.4.
DR GeneID; 100063829; -.
DR CTD; 1306; -.
DR VGNC; VGNC:16725; COL15A1.
DR GeneTree; ENSGT00940000158302; -.
DR HOGENOM; CLU_004003_0_0_1; -.
DR InParanoid; F6Q947; -.
DR OMA; RATEDQC; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000002281; Chromosome 25.
DR Bgee; ENSECAG00000021211; Expressed in synovial membrane of synovial joint and 20 other cell types or tissues.
DR ExpressionAtlas; F6Q947; baseline.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 1.
DR CDD; cd00110; LamG; 1.
DR FunFam; 3.40.1620.70:FF:000002; Collagen alpha 1 (XV) chain; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 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; IPR050149; Collagen_superfamily.
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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 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 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1388
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018611354"
FT DOMAIN 39..227
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 88..226
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 221..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..248
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..588
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..611
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..633
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..734
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1107
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1388 AA; 141038 MW; A0BBA018679E1786 CRC64;
MAPRRNGPCW RPLLLLAVSA LLPAVTRTRS ATESASQGHL DLTELIGVPL PSSVSFVTGY
GGFPAYSFGP GANVGRPART LIPPTFFRDF AISVTVKPNS ARGGVLFAIT DAFQKVIYLG
LRLSGAEDGH QRVILYYTEP GSQVSHEAAA FLVPVMTHRW NRFAVIVRGE EVSLLVDCEE
HSPVPFQRSS QPLAFEPSAG IFVGNAGATG LERFTGSIQQ LTVHPDPGTP EELCEAEESS
ASGETSGLQE TDGVAEILEA VTYTQAPSKE AQVEPISTPP TLSPPSEDAE LSGEPVPEGT
LETTKLSEPV PEGTPETTNL SVIPHSSPEQ GSGEIMNDTL EGAQTVDGAP ITDVGSGDGA
ILHVIEEGPH PEEGLATTAA AGEAEVPVST AEEAEASGVP TGGPTLSTFT EDPGERVTPG
LDTEEGSAAT AAEEAEVPIG TAGEVEADTV RTGGPTLSTS TQDPGEGVTL GPISEESLTT
AVAATEVALS TFEEEEASGV PTDGLVPLTP TVPSEQVVPS GPGDEEDLAA ATTEEPLTAA
GAEETGGALP EGPPLPIPTV APERGVTPGG AEEVLSGPPG TAEPAGPTVR AEAEGSGLAW
GLDLGSGSGS DDLVRSEELL RGPPGPPGPP GSPGIPGKPG TDIFMGPPGS PGEDGAAGEP
GPPGPEGQPG LDGASGLPGM KGEKGARGPN GSVGEKGDPG SRGLPGPPGK NGQVGTPGVM
GPPGPPGPPG PPGPGCATGL GFEDTEGSGS IRLLHEPRIS GPTASSGPKG EKGDQGPKGD
RGMDGASIVG PPGPRGPPGR IEVLPSSLIN ITHGFKNLSD IPELMGPPGP EGMPGLPGFP
GPRGPKGDTG VPGFPGLKGE QGEKGEPGTI LTGDVPLERL RGMKGEPGAH GAPGPMGPKG
PPGHKGEFGL PGRPGRPGLN GLKGAKGDRG LMMPGPPGLP GPPGPPGPPG AVINIKGAVF
PIPIRPHCKT PVGTTHPGNS ELITFHGVKG EKGSWGLPGS KGEKGDQGAQ GPPGPPVDPA
YLRHFLNSLK GENGDRGLKG EKGDSNGDFL VSGPPGLPGN PGLVGQKGET VIGPQGPPGA
PGLPGPPGFG RPGSPGPPGP PGPPGPPAIL GAAVALPGPP GPPGQPGLPG SRNLVTAFSS
MDDMLQNAHL VIEGTFIYLK DSAEFFIRVR DGWKKLQLGE LIPIPADSLP PPALSSNPHQ
PQVPLTSVSS VTYERPALHL VALNTPFSGD LRADFQCFQQ ARAAGLLSTY RAFLSSHLQD
LSTVVRKAER YSLPIVNLKG QVLFNNWDSV FSGHGGQFNT HVPIYSFDGR DVMTDPSWPQ
KAVWHGSSPR GVRLVDKYCE AWRTADTAVT GLASPLSTGK ILDQKTYSCA NRLIVLCIEN
SFMTDARK
//
