ID A0A8C4TW42_FALTI Unreviewed; 1288 AA.
AC A0A8C4TW42;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
OS Falco tinnunculus (Common kestrel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Falconiformes; Falconidae; Falco.
OX NCBI_TaxID=100819 {ECO:0000313|Ensembl:ENSFTIP00000004437.1, ECO:0000313|Proteomes:UP000694562};
RN [1] {ECO:0000313|Ensembl:ENSFTIP00000004437.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSFTIP00000004437.1}
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 Ensembl; ENSFTIT00000004651.1; ENSFTIP00000004437.1; ENSFTIG00000002940.1.
DR Proteomes; UP000694562; 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:SF1105; FIBRILLAR COLLAGEN NC1 DOMAIN-CONTAINING PROTEIN; 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:UP000694562};
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..1288
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034944345"
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..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..478
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..507
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..519
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..577
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..691
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..734
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..817
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1007
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1026
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1288 AA; 132146 MW; 9B4A8E62961C5997 CRC64;
MLSWHAWWTW GLLLLLFGCS LHAGSAAQII EERGSKGHLD LTELIGVPLP PSVYFVTGYG
GFPAYSFGPD ANIGRLTSAI VPMPFYRDFA IVVTVKPNSD RGGVLFAITD AFQKTIYLGM
RLSPVDDSTQ RIIMYYTEPG SHVSREAASF KVPVMTNRWN RFTVTVQGND VALFMDCEEY
QRVQFQRSAQ PLVFESGSGI FVGNAGATGL EKFTGSIQHL TIKSDPRATE DHCEDDDPYA
SGDISGNGSI QEHESISKTQ EVLAPSHLPI KPEDTLAEPV EAPPTVLSYL EENDFSGNHR
SEETPETAKP SAVMETGQGN SESTTVTQKI LREEGGSGAS VLPGVSKEEG QEGQEGEDKP
TGSPGSPGVE DVQKKDQGTP GRPGKLGQHS QPGKKGLQVL PGPKGRAGLK GEKGDPGEGL
PGPPGLPGPA GPPTPSGGLN RLEPEESGSG DIDRETETLR GLPGPPGPPG LPGLPGKPAP
DAGVGSPGSP GEDGAPGEPG PEGPQGPPGL DGVVGPPGQK GEKGDRGLPG SVGPKGDTGV
PGSIGLKGEA GAVGSPGKPG PPGPPGSPGP PGPPGPPGLS YNMGFEDMEG SGTISLLSES
RIPGLRGPKG SAGRHGQHGP LGPKGERGNI GPPGSKGMPG TDGKPGFPGV AGRPGDVGPK
GEKGDPGLQG EPGQNGNSIV GPPGPPGPPG PIIAIPELLL NDTEGIFNFT GIKGLLGPPG
PDGKPGLPGF PGPRGPKGDT GLPGSQGPKG QRGEKGEPGA IITADGSLTE LLGRKGEKGE
AGVVGPVGPM GPIGPTGPKG ELGFPGRPGR PGLNGLRGVK GDRGEAFNGH PGLPGPPGPP
GPPGRIIYIK GTVFPVSARP HCKMPVSTPY PGNQEALNVH GAKANGASWA LHSSPGLKGE
KGDRGAPGPP GPLLPPPYFS HFINSIKGEK GDNGVTGVKG EKGEPNGGFF LTGPPGPPGR
PGLVGPKGDS VVGPRGPPGL PGLPGLPGYG KIGPPGPPGP PGPPGPPAIY GSAAAMPGPP
GPPGEPGSPA SRNLVTTFRN IEGMLEKVHL VAEGTLIYLS ETSEVFIRVR NGWRKLQLGE
LIPIPADSLP PPAISSYGFQ SLPALSPTSN MNNGKPALHL VALNLPFSGD MRADFQCFQQ
AQLAGLTSTY RAFLSSHLQD LATVVRKTDR YHLPIVNLKG ETLFSNWESI FNGNGGQFNI
HVPIYSFDGR NVMTDPSWPQ KVIWHGSTAN GIRLVSNYCE AWHTADVGAT GQASPLKTGK
LLDQKIYSCS NQFIVLCIEN SFVSDLQG
//
