ID A0A2Y9SXG8_PHYMC Unreviewed; 1366 AA.
AC A0A2Y9SXG8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 28-JAN-2026, entry version 34.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|RefSeq:XP_007101891.2};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007101891.2};
RN [1] {ECO:0000313|RefSeq:XP_007101891.2}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007101891.2};
RG RefSeq;
RL Submitted (AUG-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_007101891.2; XM_007101829.4.
DR FunCoup; A0A2Y9SXG8; 211.
DR GeneID; 102978323; -.
DR KEGG; pcad:102978323; -.
DR CTD; 1306; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000248484; Chromosome 9.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 2.
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 ECO:0000313|RefSeq:XP_007101891.2};
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:UP000248484};
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..1366
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5043769640"
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..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1108
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..437
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..611
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..710
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..821
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..901
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..927
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1023
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1042
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1085
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1366 AA; 139457 MW; 2820F43FC0FB560D CRC64;
MAQRRDTQCW RLLWLLSISA LLPAVTRTRS ATELASQGHL DLTELIGVPL PSSVSFVTGH
GGFPAYSFGP GANVGRPART LMPPTFFRDF AISVMAKPSS ARGGVLFAIT DAFQKVIYLG
LRLSGVEDGS QRVILYYTEP GSKVSREAAA FPVPVMTHRW NRFAMVVQGE EVTLLVDCEE
HSHVPFPRSS RLLAFEPSAG IFIGNAGATG LERFTGSIQQ LTIHRDPGTP EELCEAEESS
ASGETSGLQE TDRVAEILEA VTYTQAPSRE ARVGPINTPP TLSSPSEDAE LSGEPVPEGA
QETTNMSAVP HSSPKQGSGE ILNDTLETVD TVDGSPITDT GSGDGAFLHV IEEGPYMEEG
LTATAAAGQA EVSISTAREA EAGSVPTEGL TLSMSTKHPG EGVTLGPDNE EGSAATAAGE
TEVPVSSAGE AEASSVPTGG LTLSMPTQDP GEGVTLGPIS EESLTIAAAA AKVPLSTFEE
EEASGFPTDG LVPLTPTAAP KQVVTSGPGD EDVAAATTEQ PLPAAGAEEL GGALPEGPPL
PIPTVAPERG VPPGEAEEGL PGPLGPAGPT VGVEAEGSSL GRGLDVGSGD PVRSEELLRG
PPGPPGPPGL PGIPGKPGTD VSMGPPGSPG EDGPAGEPGP PGPQGKPGLD GASGLPGMKG
EKGARGPNGS FGEKGDPGNR GLPGPPGKNG QVGIPGVMGP PGPPGPPGPR GPGCAMGLGF
EDTEGSGSVR LLHEPRISGP MASSGPKGEK GDQGPKGERG MDGASIVGPP GPRGLPGRIE
VLSSPLINIT HGFMNLSDIP ELVGPPGPEG TPGLPGFPGP RGPKGDTGVP GFPGLKGEQG
EKGEPGAILT GDIPLERLRS RKGEPGEHGA PGPMGPKGPP GHKGEFGLPG RPGRPGLNGL
KGTKGDRGVM MPGPPGLPGP PGPPGPPGAV INIKGAVFPV PVRPHCKTPV GTTYPGNSEL
ITFHGVKGEK GSWGLPGSKG EKGDQGAQGP PGPPVDPTYL RHFLNSLKGE NRDRGIKGEK
GDSDSGFSVS GPPGLPGSPG LAGQKGETIV GPQGPPGAPG LPGPPGFGIP GSPGPQGPPG
PPGPPAILGA AVAIPGPPGP PGQPGLPGSR NLVTAFSNMA DMLQKAHLVI EGTFIYLKDS
TEFFIRVRDG WKKLQLGQLI PIPDDSPPPP ALSSNSHQLQ LPLASISSVN YDSPALHLVA
LNTPFSGDIR ADFQCFQQAR AAGLLSTYEA FLSSHLQDLS TVVRKAERYS LPIVNLKGQV
LFNNWDSIFS GHGGQFNTHV PIYSFDGRDV MTDPSWPQKV VWHGSSTHGV RLVDQYCEAW
RTADMAVMGL ASPLSTGKIL DQKAYSCANR LIVLCIENSF MTDARK
//
