ID A0A340XNK0_LIPVE Unreviewed; 1366 AA.
AC A0A340XNK0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|RefSeq:XP_007461712.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007461712.1};
RN [1] {ECO:0000313|RefSeq:XP_007461712.1}
RP IDENTIFICATION.
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_007461712.1; XM_007461650.1.
DR FunCoup; A0A340XNK0; 216.
DR STRING; 118797.A0A340XNK0; -.
DR GeneID; 103072227; -.
DR KEGG; lve:103072227; -.
DR CTD; 1306; -.
DR InParanoid; A0A340XNK0; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000265300; Unplaced.
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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1077; COLLAGEN ALPHA-3(IV) CHAIN; 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_007461712.1};
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:UP000265300};
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_5016346763"
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..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1109
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 854..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..901
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..925
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1022
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; 139601 MW; 30C0BF7287807316 CRC64;
MAQRRDTQCW RLLWLLSTSV LLPAVTRTRS ATELASQGHL DLTELIGVPL PSSVSFVTGY
GGFPAYSFGP GANVGRPART LIPPTFFRDF AISVMAKPSS ARGGVLFALT DAFQKVIYLG
LRLSGVEDGS QRVILYYTEP GSKVSHEAAA FPVPVMTHRW NRFAMVVQGE EVTLLVNCEE
HSHVPFPRSS RALAFEPGAG IFVGNAGATG LERFTGSIQQ LIIHRDPRTP EELCEAEESS
ASGETSGLQE TDRVAEILEA VTYTQAPSRE ARVGPINTPP TLSSPSEDAE LSGEPVPEAA
QETTNMSAVP HSSPKQGSGE ILNDTLETVD TVDGSPITDT GSGDGNFLHV TEEGPHMEEG
LAATAAAGEA EVSISTAREA EAGSVPTEGL TLSMSTKHPG GGVTLGPDNE EGSAATAAGE
AEVPVSSAGE AEASSVPTGG LTLSMPTQDP GEGVTLGPTS EESLTIAAAA AKVPLSTFEE
EEASGFPTDG LVPLTPTAAP KQVVTSGPGD ENLAAATTEQ PLPTAGAEEL GGTLPEGPPL
PIPTVAPERG VPPGEAGEGL PDPLGPAGPT VGVEAEGSSL GWGLDVGSGD PVPSEELLRG
PPGPPGPPGL PGIPGKPGTD VFMGPPGSPG EDGPAGEPGP PGPEGKPGLD GASGLPGMKG
EKGARGRNGS FGEKGDPGNR GLPGPPGKNG QVGAPGVMGP PGPPGPPGPR GPGCTMGLGF
EDTEGSGNIR LLHEPRISGP TASSGPKGEK GDQGPKGERG MDGASIVGPP GPRGLPGRIE
VLSSPLINIT HGFMNLSDIP ELVGPPGPEG MPGLPGFQGP RGPKGDTGVP GFPGLKGEQG
EKGEPGAILT GDIPLERLRT RKGEPGERGA PGPMGPKGPP GHKGEFGLPG RPGRPGLNGL
KGAKGDRGVV MPGSPGLPGP PGPPGPPGAV INIKGAVFPV PVRPHCKTPV GTTYPGNSEL
ITFHGVKGEK GSWGLPGSKG DKGDQGAQGP PGPAVDPTYL RHFLNSLKGE NRDRGIKGEK
GDSNSGFSVS GPPGLPGSPG LEGQKGETIV GPQGPPGAPG LPGPPGFGRP GSPGPQGPPG
PPGPPAILGA AVAIPGPPGP PGQPGLPGSR NLVTAFSNMA DMLQKAHLVI EGTFIYLKDS
TEVFIRVRDG WKKLQLGELI PIPDDSPPPP ALSSNSHQLQ LPLASISSVN YESPALHLVA
LNTPFSGDVR ADFQCFQQAR AAGLLSTYEA FLSSHLQDLS TVVRKAERYS LPIVNLKGQV
LFDNWDSIFS GHGGQFNTHV PIYSFDGRDV MTDPSWPQKV VWHGSSTYGV RLVDQYCEAW
RTADMAVMGL ASPLSTGKIL DQKAYSCANR LIVLCIENSF MTDVRK
//
