ID A0A667GVZ9_LYNCA Unreviewed; 1352 AA.
AC A0A667GVZ9;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSLCNP00005019307.1};
OS Lynx canadensis (Canada lynx) (Felis canadensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Lynx.
OX NCBI_TaxID=61383 {ECO:0000313|Ensembl:ENSLCNP00005019307.1, ECO:0000313|Proteomes:UP000472241};
RN [1] {ECO:0000313|Ensembl:ENSLCNP00005019307.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSLCNP00005019307.1}
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_032451426.1; XM_032595535.1.
DR Ensembl; ENSLCNT00005021628.1; ENSLCNP00005019307.1; ENSLCNG00005012560.1.
DR GeneID; 115499365; -.
DR CTD; 1306; -.
DR Proteomes; UP000472241; 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: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: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 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:UP000472241};
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..1352
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025589173"
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 222..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..477
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..574
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..698
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..887
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1071
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1090
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1352 AA; 137817 MW; 2C2AA6E41CA474B9 CRC64;
MAPRRNGRWW PLLLLLSVSA LLPSVTRTRS ATESLSPGHL DLTELIGVPL PSSVSFVTGY
GGFPAYSFGP GANVGRPART LIPPTFFRDF AITVTVKPSS ATGGVLFAIT DAFQKVIYLG
LRLSGVEDGR QRIILYYTEP GSHVSHEAAA FLVPVMTHRW NRFAVIVQGE EVTLFMDCEE
HSHVPFQRSS RALAFEPSAG IFVGNAGATG LERFTGSIQQ LTVHPDPRTP EELCEADESS
GSGETSGLQE TEGVAEILEA VTYTQAPSKE AKVEPINTPP TPSTPSDDGE LSGEPVPEGT
PETTNLSVIL HSSPEQGSGE ILNDTLEGVH TVDGAPVTDV GSGDGTLIHV TEESVHTEEG
LAATAAAGEA EVPISTAGEA EASSAPTGGP ALSLSTEDMG EGVTPGADAE EGSAATAAEE
AEVPISTAGE VEAGSVPTAE VTLSVSTQGP GERVTLGPVG EETLTTAAAA AEASLSTSEE
EEARGVPTDG LAPLAPTAAP EQEVTSGPGD EEDLAAASTE EPIPVAVAEE LDSTLPEGPP
LPVPTVASER TVTPVSAEAE GSGLGWGSDI GSGSGDLVRT EELLRGPPGP PGPPGSPGIP
GKPGTDVFMG PPGSPGKDGA AGEPGPPGPE GQPGPDGASG LPGMKGEKGA RGPNGSAGEK
GDPGSRGLPG PPGKNGQVGA PGVMGPPGPP GPPGPPGPGC AMGLGFEDTE GSGSIRLLHE
PRISGPAVSS GPKGEKGDQG PKGDRGMDGA SIVGPPGPRG PPGRIEVLSS SLVNITHGFL
NLSDIPELIG PPGPEGIPGL PGFPGPRGPK GDTGVPGFPG LKGEQGEKGE PGAILTGDIP
LERLQGRKGE PGVHGAPGPM GPKGPPGHKG EFGLPGRPGR PGLNGLKGAK GDRGVMMLGP
PGLPGPPGPP GPPGAVINIK GAVFPIPVRP HCKTPVDTTH PGNSELITFH GVKGEKGSWG
LPGSKGEKGD QGAQGPPGPP VDPTYLRYLL NSLKGENGDR GIKGEKGDSH GDFFVSGPPG
LPGSPGLVGQ KGETVVGPQG PPGAPGLPGP PGFGRPGSPG PPGPPGPPGP PAILGAAVAL
PGPPGPPGQP GLPGSRNLVT AFSSMDDMLQ KAHLVIEGTF IYLRDSTDFF IRVRDGWKKL
QLGELIPIPE DSPPPPALSS NPHQPQPPLM SLSSVNYQRP ALHLVALNTP FSGDIRADFQ
CFQQARAAGL LSTYRAFLSS HLQDLSTVVR KAERYSLPIV NLKGQVLFNN WDSIFSGHGG
QFNTHVPIYS FDGRDVMTDP SWPQKVIWHG SSTHGVRLVD KYCEAWRTAD MAVMGLASPL
STGKILDQKA YSCANRLIVL CIENSFMTDA RK
//
