ID A0A8C9BNE2_PHOSS Unreviewed; 1364 AA.
AC A0A8C9BNE2;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSPSNP00000012987.1};
OS Phocoena sinus (Vaquita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Phocoenidae; Phocoena.
OX NCBI_TaxID=42100 {ECO:0000313|Ensembl:ENSPSNP00000012987.1, ECO:0000313|Proteomes:UP000694554};
RN [1] {ECO:0000313|Ensembl:ENSPSNP00000012987.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Morin P., Mountcastle J., Fungtammasan C., Rhie A., Rojas-Bracho L.,
RA Smith C.R., Taylor B.L., Gulland F.M.D., Musser W., Houck M., Haase B.,
RA Paez S., Howe K., Torrance J., Formenti G., Phillippy A., Ryder O.,
RA Jarvis E.D., Fedrigo O.;
RT "Phocoena sinus (Vaquita) genome, mPhoSin1, primary haplotype.";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPSNP00000012987.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSPSNP00000012987.1}
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 RefSeq; XP_032492084.1; XM_032636193.1.
DR Ensembl; ENSPSNT00000014700.1; ENSPSNP00000012987.1; ENSPSNG00000009563.1.
DR GeneID; 116756023; -.
DR CTD; 1306; -.
DR GeneTree; ENSGT00940000158302; -.
DR Proteomes; UP000694554; Chromosome 6.
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 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:SF912; COLLAGEN ALPHA-1(XV) CHAIN; 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:UP000694554};
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..1364
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034155016"
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 263..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1104
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 412..440
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..533
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..609
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..708
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..899
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1040
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1083
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1364 AA; 139684 MW; BDFD29E50D0D0D05 CRC64;
MAQRRDTQCW RLLWLLSISV LLPAVTRTRS ATELASQGHL DLTELIGVPL PSSVSFVTGY
GGFPAYSFGP GANVGRPART LIPPIFFRDF AISVMVKPSS ARGGVLFAIT DAFQKVIYLG
LRLSGVEDGS QRVILYYTEP GSKVSHEAAA FPVPVMTHRW NRFAMVVQGE EVTLLVGCEE
HSHIPFPRSS RVLAFEPSAG IFVGNAGATA LERFTGSIQQ LTIHRDPRTP EELCEAEESS
ASGETSGLQE TDRVAEVLEA VTYTQAPSRE ARVGPINTPP TLSSPSEDAE LSGEPVPEGP
QETTTMSAVP HSSPKQGSGE ILNDTLETVD TVDGSPITDT GSGDGAFLHV TEEGPHMEEG
LAATAAAGEA EVSISTAREA EAGSVPTEGL TLSMSTEHPG EGVTLGPDNE EGSAATATGE
AEVPVSSAGE AEASSVPSGG LTLSMPTQDP GEGVTLGPIS EESLTIATAK VPLSTFEEEE
ASGFPTDGLV PLTPTAAPKQ VVTSGLGDED LAAATTEQPL PMAGAEELGG ALPEGPPLPI
PTVAPERGVP PGEAGEGLPD PLGPAGPTVG VEAEGSSLGW GLDVGSGDPV PSEELLRGPP
GPPGPPGLPG IPGKPGTDVF MGPPGSPGED GPAGEPGPPG PEGKPGLDGA SGLPGMKGEK
GARGRNGSFG EKGDPGNRGL PGPPGKNGQV GAPGVMGPPG PPGPPGPRGP GCTMGLGFED
TEGSGSIRLL HEPRISGPTA SSGPKGEKGD QGSKGERGMD GASIVGPPGP RGLPGRIEVL
SSPLINITHG FMNLSDIPEL IGPPGPEGMP GLPGFQGPRG PKGDTGVPGF PGLKGEQGEK
GEPGAILTGD IPLERLRTRK GEPGERGAPG PMGPKGPPGH KGEFGLPGRP GRPGLNGLKG
AKGDRGVMMP GSPGLPGPPG PPGPPGAVIN IKGAVFPVPV RPHCKTPVGT TYPGNSELIT
FHGVKGEKGS WGLPGSKGEK GDQGAQGPPG PAVDPTYLRH FLNSLKGENR DKGIKGEKGD
SDSGFSVSGP PGLPGSPGLA GQKGETIIGP QGPPGAPGLP GPPGFGRPGS PGPQGPPGPP
GPPAILGAAV AIPGPPGPPG QPGLPGSRNL VTAFSNMADM LQKAHLVIEG TFIYLKDSTE
FFIRVRDGWK KLQLGELIPI PDDSPPPPAL SSNSHHLQLP LASISSVNYE RPALHLVALN
TPFSGDIRAD FQCFQQARAA GLLSTYEAFL SSHLQDLSTV VRKAERYSLP IVNLKGQVLF
DNWDSIFSGH GGQFNTHVPI YSFDGRDVMT DPSWPQKVVW HGSSTHGVRL VDQYCEAWRT
ADMAVMGLAS PLSTGKILDQ KAYSCANRLI VLCIENSFMT DVRK
//
