ID A0A6J2ITV1_9PASS Unreviewed; 1290 AA.
AC A0A6J2ITV1;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=LOC114001849 {ECO:0000313|RefSeq:XP_027603196.2};
OS Pipra filicauda (Wire-tailed manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Pipridae; Pipra.
OX NCBI_TaxID=649802 {ECO:0000313|Proteomes:UP000504627, ECO:0000313|RefSeq:XP_027603196.2};
RN [1] {ECO:0000313|RefSeq:XP_027603196.2}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_027603196.2};
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_027603196.2; XM_027747395.2.
DR GeneID; 114001849; -.
DR InParanoid; A0A6J2ITV1; -.
DR Proteomes; UP000504627; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 4.
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:UP000504627};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1290
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030157323"
FT DOMAIN 38..226
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 87..225
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 223..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..481
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..502
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..520
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..580
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..677
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..692
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..735
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..752
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..818
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..844
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..917
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1008
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1027
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1290 AA; 133018 MW; A0AD25BF59032AD9 CRC64;
MLSWHAWWTW DSLLLLFGLS IHAGSAAQII EERGSKGHLD LTELIGVPLP PSVYFVTGYG
GFPAYSFGPD SNIGRLTSAI IPSPFYRDFA IIVTVKPNSD RGGVLFAITD AFQKTIYLGL
RISPVDDSTQ RIIMYYTEPG SHISREAASF KVPVMTNRWN RFTVTVQEND VALFMDCEEY
QRLQFQRSTR TLVFESGSGI FVGNAGATGL EKFTGSIQHL TIKSDPRATE DHCEDDDPYA
SGDSSGNGSI QEHEVSEAQG VLSPSHLPMR PEDTLAEPVE APPTILSYLE ENDFSGNQRS
EETSEAAKLK EQDSSVMETG QGNSESTTVM QKILREEDGS AAGVLPEVSG EEGQKGQEVE
DGSTGSLGGS GAEDLQKKGQ GPPGPPRKLG QLDHPGKNRH QELPGLKGKA GLKGEKGDPG
EGLPGPPGLP GPAGPSAPSR GLNRLEPEES GSGDNDRETE ILIGLPGPPG PPGLPGLPGK
PAPDSGVGPP GSPGEDGASG EPGPEGPQGP PGRDGVVGPP GWKGEKGDQG LPGSVGPKGD
TGVTGSIGPK GEAGALGSPG KPGPPGPPGP PGPPGPPGPP GLSYSLGFED MEGSGSLLSE
SRIPGSKRPK GSAGRQGQRG PLGPKGERGN TGLPGSKGMP GTDGKPGFPG IAGHPGGVGP
KGEKGDPGPQ GEPGENGNSI VGPPGPPGPP GPVIAIPELL LNDTNGMFNF TVIKGLLGPP
GPDGKPGPPG FPGPRGPKGD TGLPGSQGPK GQQGEKGEPG AIIAADGSLT ELIGRKGEKG
EAGVVGPAGP MGPIGPTGPK GELGFPGRPG RPGLNGLRGV KGDRGEAFNG PPGLPGPPGP
PGPPGRILYI KGTVFPVPPR PHCKMPVSTP YPGNQEPLNE YGAKANRDSW GLHSSAPLKG
EKGDRGAPGP PGPPLPPSYF SHFINSIKGE KGDNGVTGVK GEKGEPNGGG FLTGPPGPPG
RPGLVGPKGD SVVGPRGPPG LPGLPGLPGY GKIGPPGPPG PPGPPGPPAI YGSAAAMPGP
PGPPGEPGSP ATRNLVTTFQ NIEGMLEKVH FVAEGTLIYL RETSEVFIRV RNGWRKLQLG
ELIPIPADSL PPPAISSHGF QSIPALRPVS NMNNGKPALH LVALNFPFSG DMRADFQCFQ
QAQLAGLTST YRAFLSSHLQ DLATVVRKTD RYHLPIVNLK GETLFSNWES IFDGNGGQFN
IHVPIYSFDG RNIMTDSSWP QKVIWHGSTA NGIRLVSNYC EAWHTADMGA MGQASPLKTG
KLLDQKVYSC NNQFIVLCIE NSFVSDPQGK
//
