ID A0A2Y9FYJ2_TRIMA Unreviewed; 1363 AA.
AC A0A2Y9FYJ2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 28-JAN-2026, entry version 32.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|RefSeq:XP_012409829.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_012409829.1};
RN [1] {ECO:0000313|RefSeq:XP_012409829.1}
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_012409829.1; XM_012554375.2.
DR FunCoup; A0A2Y9FYJ2; 213.
DR STRING; 127582.A0A2Y9FYJ2; -.
DR GeneID; 101352770; -.
DR KEGG; tmu:101352770; -.
DR CTD; 1306; -.
DR InParanoid; A0A2Y9FYJ2; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-ARBA.
DR GO; GO:0005594; C:collagen type IX trimer; IEA:TreeGrafter.
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:SF372; COLLAGEN ALPHA-1(XVI) 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_012409829.1};
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:UP000248480};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1363
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016138799"
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 265..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..618
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..719
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..892
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..917
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1017
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1080
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1099
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1363 AA; 140367 MW; F39D955CE0477BBF CRC64;
MAPRRNRQCW RLLLLLSVSA LLSAVTRTRA LTELASQGHL DLTELIGVPL PSSVSFVTGY
GGFPAYSFGP GANIGRPART LIPPTFFRDF AIGVMVKPSS TQGGVLFAIT DAFQKVIYLG
LRLSGVEDGR QRIILYYTEP GSHVSREAAV FLVPVMTHRW NRFAVIVQGE EVALLMDCEE
HSHVAFQRSS QALGIEPSAG IFVGNAGATG LERFTGSIQQ LTIHADPRAP EELCEAEESS
ASGETSGLQE TDGVAEILEA ITYTQAPPRE AKVEPINAPP TPTSPSEDVE LSGEPVPEKT
PEATHLSGVV HSISEQGSGE ILDVTSEEVH TVDGDPITGS GSGDGDFLGV MEEKGPHTEG
LAATAAAGEA EGPVNTTWEA EASSVLTEGP TLSMSTEKPE EWVTPGPDNE ESLTATVAGE
TELSVSSAGE AEVGSVPTQG LALSTSTENL GEEATLGPNG EESWTTAAAT IEAPLSTAEE
EETSRAPTDR LAFLTPTAAL GQGNASGPDD EDDLSAAREE PLTMAWGEES GSAPPGGPPL
PIPTAAPERA VSPDDAGEEL PGSFEPAEPI RPTVGAEAEG FDLAWGSGLD LGSGSGDLVH
SEDLLRGPPG PPGPPGLPGI PGKPGADVFM GTPGSPGKDG AAGEPGPPGP EGEPGLNGAS
GLPGMKGEKG ARGPNGSVGE KGDPGDRGLP GPPGKNGQVG SPGLMGPPGP PGPPGPPGPG
CAIGLGFEDT EGSGSIRLLS EPSVSPPTAS CGLKGEKGDQ GPKGDRGLDG ASIVGPPGPR
GPPGHIKVLS SALINITHGF MNFSDIPELI GPPGPRGPKG DTGIPGFPGL KGEQGEKGEP
GTILTGDIPV ERLRGRKGEP GVHGTPGPMG PKGPPGRKGE FGFPGRPGRP GLNGLKGAKG
DRGVMMPGPP GLPGPPGPPG PPGAVINIKG AIFPIPARPH CKMPVGTTHP GNSELITFHG
VKGEKGSWGL PGSKGEKGDQ GAQGPPGPPV DPTYLRHFLN SLKGENGDRG FKGEKGDSNG
NFFVPGPPGL PGSPGLVGQK GEMIIGPQGP PGAPGLPGPP GFGRPGTPGP PGPPGPPGPP
AILGAAVPLP GPPGPPGQPG LPGSRNLVTA FSNMDDMLQK AHLVIEGTFI YLRDSTEFFI
RVREGWKKLQ LGELIPIPAD SPPPPALSSN PRQHQPQPPL TPILSANYEK PALHLVALNT
PFSGYIRADL QCFQQARAAG LLSTYRAFLS SHLQDLSTIV RKAERYSLPI VNLRGQVLFN
NWDSIFSGHG GQFNTRVPIY SFDGRDVMTD PSWPQKIIWH GSNVHGVRLV DNYCEAWRTE
DMAVTGFASP LSTGKILDQK AYSCASRLIV LCIENSFMTD ARK
//
