ID A0A452G6U2_CAPHI Unreviewed; 1363 AA.
AC A0A452G6U2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSCHIP00000032275.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000032275.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000032275.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000032275.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCHIP00000032275.1}
RP IDENTIFICATION.
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 EMBL; LWLT01000007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSCHIT00000040150.1; ENSCHIP00000032275.1; ENSCHIG00000026298.1.
DR GeneTree; ENSGT00940000158302; -.
DR Proteomes; UP000291000; Chromosome 8.
DR Bgee; ENSCHIG00000026298; Expressed in longissimus thoracis muscle and 17 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-ARBA.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF966; COLLAGEN ALPHA-1(XXII) CHAIN-LIKE; 1.
DR Pfam; PF01391; Collagen; 2.
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 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:UP000291000};
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..1363
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019166188"
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 230..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..543
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..553
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..615
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..716
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..892
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..918
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1029
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1082
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1363 AA; 139292 MW; 08DB2050FEEE6C84 CRC64;
MAPRRDAQCW RLLLLLSTSA LLPGVTRTRS ATESASRGPL DLTELIGVPL PSSVSFVAGY
GGFPAYSFGP GANVGRPART LIPSTFFRDF AISVRVKPSS PRGGVLFAVT DAFQKVIYLG
LRLSGVEDGQ QRVILYYTEP SSQVSHEAAA FLVPVMTHKW NYFAVVIQGE EVTLLVDCEE
HGRVPFPRSS QALTFEPSAG IFVGNAGATG LERFTGSIQQ LIIHPDPRTP EEMCEAEESS
ASGETSGLQE TDEVAEILEA VTYTQAPSKE AKVEPIHTPP TPSPAPEDAE LSGEPIPEGT
KETSNLSADP HSSPEQGSGE ILNDTLETVQ TVDGSPATDT GSGDGAFLRV TEESPYTEDL
AATAAAREAK TPISTAREAE ASSVPTGGLT LSMSIEHPGE GVTLAPENEE GSAATAAGEA
EEPVSIAREA EASSVPTGGL TLPMPTQDPG ETVTLSPIRE EGSTTAAAAA DVPLGAFEEE
EASGVPTDDL AFVTPTVASE QGVTLGPGDE DLAAVTTEEP LTAAGADALG STPPEGPPLP
LPSVAPERGT PPGEAEEGFP GPPGPAGPTE PTVEMEAEGS GLGWGLDVSS GSGDLVPSEE
LLRGPPGPPG PPGLPGIPGK PGTDVFMGPP GSPGEDGPTG EPGPPGPEGK AGLDGASGLP
GMKGEKGARG PNGSVGEKGD PGNRGLPGPP GKNGQVGAPG VMGPPGPPGP PGPPGPGCTT
GLVFEDAEGS GSIRHLHEPI SGPTASSGPK GEKGDRGPKG DRGMDGASIV GPPGPRGPPG
RIEVLSSSLT NITQGFMNFS DIPELVGPPG PRGPKGDTGV PGFPGLKGEQ GEKGEPGAIL
TGDVPLERLR GQKGEPGEHG APGPMGPKGP PGHKGEFGLP GRPGRPGLNG LKGAKGDRGV
MIPGPPGLPG PPGPPGPPGA VINIKGAVFP IPVRPHCKTP VGTTYSGNSE LITFHGVKGE
KGSWGLPGSK GEKGDQGPQG PPGPPVDPAY LRHFLNSLKG ENGDRGLKGE KGDSNSGFSG
FSGFSASGPP GLPGSPGLVG QKGEAVVGPQ GPPGAPGLPG PPGFGRPGSP GPPGPPGPPG
PPAILGAAVA LPGPPGPPGQ PGLPGSRNLV TTFSNMDDML QKAHLVIEGT FIYLKDSTEF
FIRVRDGWKK LQLGELIPIP DDSPPPPALS SNPHQPQLSL TSISNVNYDR PALHLVALNT
PFSGDIRADF QCFQQARAAG LLSTYRAFLS SHLQDLSTVV KKAERYSLPI VNLKGQVLFN
NWDSIFSGHG GQFNTHVPIY SFDGRDVMTD PSWPQKVVWH GSSTHGVRLV DQYCEAWRTA
DMAVMGLASP LNTGKILDQK AYSCANRLIV LCIENSFMTD ARK
//
