ID A0A7K9WR15_9PASS Unreviewed; 1328 AA.
AC A0A7K9WR15;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 08-OCT-2025, entry version 16.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
DE Flags: Fragment;
GN Name=Col15a1_1 {ECO:0000313|EMBL:NXI87515.1};
GN ORFNames=RHIDAH_R11094 {ECO:0000313|EMBL:NXI87515.1};
OS Rhipidura dahli.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Rhipiduridae; Rhipidura.
OX NCBI_TaxID=667186 {ECO:0000313|EMBL:NXI87515.1, ECO:0000313|Proteomes:UP000561178};
RN [1] {ECO:0000313|EMBL:NXI87515.1, ECO:0000313|Proteomes:UP000561178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-001-49 {ECO:0000313|EMBL:NXI87515.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXI87515.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NXI87515.1}.
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DR EMBL; VXAC01007861; NXI87515.1; -; Genomic_DNA.
DR Proteomes; UP000561178; Unassembled WGS sequence.
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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1118; LAMININ G DOMAIN-CONTAINING PROTEIN; 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:UP000561178};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 8..196
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 57..195
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 193..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..568
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..589
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..667
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..733
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..776
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..793
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..958
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1049
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1068
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXI87515.1"
FT NON_TER 1328
FT /evidence="ECO:0000313|EMBL:NXI87515.1"
SQ SEQUENCE 1328 AA; 140092 MW; F268ABDB7FBBFB20 CRC64;
TERGSKGHLD LTELIGVPLP PSVYFVTGYG GFPAYSFGPD SNIGRLTSAI IPSPFYRDFA
VVVTVKPNSD RGGVLFAITD AFQKTIYLGL RISPVDDSTQ RIIMYYTEPG SHISREAASF
KVPVMTNRWN RFTVTVDGNE VALFMDCEEY QRLQFQRSAR TLAFESGSGI FVGNAGATGL
EKFTGSIQHL TIKSDPRATE DHCEDDDPYA SGDSSGNGSI QEHDVSEAQE ALGSSRLPIG
PEDTLAEPVE APPTILSYME ENDFSGNHRS EETSEAAKFK EQGTASAVME TGRDNSESTP
VTQKVLREED GSGAGVLTGV SREEVYNSHP WVSSPQAAGS LHTYPLCSLS RRFIIKGCGC
RRPARGCETQ PKAAQRRERE REGVQAPGNG RALRAQRMQR IKNAESKKVI IFIRLSYFIF
PSSTCSQNQE AWETNRGTYT SMHSLRATTS ERLQRHGGTA HSWSATMDGY RFFRKDRLGR
QIIKLFLPLP MQRSCFLERV LEMDKVQPCS QHLSSHSCDW KSTQIAASAY SLYMVKSLLI
YLNSHFRVIL GLPGPPGPPG LPGLPGKPAP DSGVGPPGSP GEDGASGEPG PEGPQGPSGR
DGVVGPPGWK GEKGDQGLPG SAGPKGDTGV TGSIGPKGEA GPIGSPGKPG PPGPPGPPGP
PGPPGPPGLS YSLGFEQGRG NFTISSFKSL ILIFFYHLQG PKGEKGDPGP RGEPGQDGNS
IVGPPGPPGP PGPIIAIPEL LLNDTDGIFN FTEIKGLLGP PGPDGKPGLP GFPGPRGPKG
DTGLPGSQGP KGQQGEKGEP GAIISADGSL TELLGRKGEK GEAGVVGPAG PMGPIGPAGP
KGELGFPGRP GRPGLNGLRG VKGDRGEAFN GLPGLPGPPG PPGPPGRILY IKGVIFPVPP
RPHCKVPVNT PYPGNQEVLN YHGAKANRDS WGLHSSAHLK GEKGDRGAPG PPGPPLPPSY
FSHFINSIKG EKGDNGVTGV KGEKGEPNGG FFLTGPPGPP GRPGLIGPKG DSVVGPRGPP
GLPGLPGLPG YGKIGPPGPP GPPGPPGPPA IYGSAAAMPG PPGPPGEPGS PATRNLVTTF
QNIEGMLEKV HYVAEGTLIY LRETSEVFIR VRNGWRKLQL GELIPIPADS LPPPAISSHG
FQSIPALRPI SNMNHGKPAL HLVALNFPLS GDMRADFQCF RQAQLAGLTS TYRAFLSSHL
QDLATVVRKT DRHHLPIVNL QGETLFSNWE SIFDGNGGQF NIHVPIYSFD GRNVMTDSSW
PQKVVWHGST ADGIRLVSSY CEAWHAAGMG ATGQASPLNT GKLLDQKVYS CNNQFIVLCI
ENSFVSDP
//
