ID A0A2Y9J7T9_ENHLU Unreviewed; 1382 AA.
AC A0A2Y9J7T9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-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=LOC111145762 {ECO:0000313|RefSeq:XP_022356656.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022356656.1};
RN [1] {ECO:0000313|RefSeq:XP_022356656.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022356656.1};
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_022356656.1; XM_022500948.1.
DR STRING; 391180.A0A2Y9J7T9; -.
DR GeneID; 111145762; -.
DR KEGG; elk:111145762; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000248482; 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 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 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 ECO:0000313|RefSeq:XP_022356656.1};
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:UP000248482};
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..1382
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016106206"
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..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..440
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..486
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..603
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..629
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..730
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..839
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..919
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1060
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1103
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1122
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1382 AA; 140169 MW; 6D5D9E8AE13B0E28 CRC64;
MAPRRNARCW RLLLLLSISA LLPAVSQTRS ATDLASQGHL DLTELIGVPL PSSVSFVTGY
GGFPAYSFGP GANVGRPART LIPPTFFRDF AISVTVKPSS DNGGVLFAIT DAFQKIIYLG
LRLSGMEDGR QRVILYYTEP GSHVSHEAAA FPVPVMTHRW SRFSVIVQGE EVALLMDCEE
HGHIPFQRSS RPLAFEPSAG IFVGNAGATG LERFTGSIQQ LTVHPDPRIP EELCESEESS
ASGEASGLQD TEGVAEILEA VTYTQAPSKE AEVEPINTPP IPSPPSDDAE LSGELVSEGT
LETTNLSITE HSGLEQGSGE VLNDTLEGVH TMDGAPVTDG APITDGAPGT DVGSGGGAFI
HVTEESVRAE EGLAATAAVG KAELPPSPTG EAEASSVPTG GPALSLSTED TGEGVTLGAD
AEEGSAATAA GEAGSTAGEV EASRVPAGGV TPSMPIQDAG EGITWGATGE AMFTTPAAAA
EVTPSTSEEE ETRGVPTGGL APPTPTVAPE QAVASGSGEE EDLAAAATRE PLPGTVAEEL
DGSPPEGPPL SIPTVASERG VTLAEAGEGL PGHPEPARPT RPTVGAEAEG SGLGWGLDVG
SGSGDLVRSE ELLRGPPGPP GPPGPPGSPG IPGKPGTDVF MGPPGSPGED GAAGEPGPPG
PEGQPGADGA SGLPGMKGEK GARGPNGSVG EKGDPGNRGL PGPPGKNGQV GSPGVMGPPG
PPGPPGPPGP GCTAGLGLED PEGSGSIRLL HEPGLSGPVA PSGPKGEKGD QGPKGDRGMD
GASIVGPPGP RGPPGRIEVL SSSLTNLTHG FMNLSDIPEL AGPPGPEGIP GLPGFPGPRG
PKGDTGVPGF PGLKGEQGEK GEPGAILTGD IPLERLQGKK GEPGEHGAPG PMGPKGPPGH
KGEFGLPGRP GRPGLNGLKG AKGDRGIMMP GPPGLPGPPG PPGPPGAVVN IKGAVFPIPV
RPHCKTPVDT THPGNSELIT FHGIKGEKGS WGLPGSKGEK GDQGAQGPPG PPVDPAYLRH
FLNSLKGENG DQGIKGEKGD SHSDFSVSGP PGLPGSPGLV GQKGETVIGP QGPPGAPGLP
GPPGFGRPGS PGPPGPPGPP GPPAILGAAV ALPGPPGPPG QPGLPGSRNL VTAFSTMDDM
LQKAHLVIEG TFIYLRDSTE FFIRVRDGWK KLQLGELIPI PADSPPPPAL SSNPHPPPLM
PISSVSYERP VLHLVALNTP FSGDFRADFQ CFQQARAAGL LSTYRAFLSS HLQDLSTVVR
KAERYSLPIV NLKGQVLFNN WDTIFSGHGG QFNTHIPIYS FDGRDVMTDP SWPQKVIWHG
SSPHGVRLVD NYCEAWRTAD MAVTGLASPL STGKILDQKT YSCANRLIVL CIENSFMTDA
RK
//
