ID A0A7K8AKV5_9CORV Unreviewed; 1307 AA.
AC A0A7K8AKV5;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
DE Flags: Fragment;
GN Name=Col15a1_1 {ECO:0000313|EMBL:NXB03324.1};
GN ORFNames=CNELOR_R13006 {ECO:0000313|EMBL:NXB03324.1};
OS Cnemophilus loriae (Loria's bird-of-paradise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Corvoidea; Corvidae; Cnemophilus.
OX NCBI_TaxID=254448 {ECO:0000313|EMBL:NXB03324.1, ECO:0000313|Proteomes:UP000517678};
RN [1] {ECO:0000313|EMBL:NXB03324.1, ECO:0000313|Proteomes:UP000517678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-029-38 {ECO:0000313|EMBL:NXB03324.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXB03324.1};
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:NXB03324.1}.
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DR EMBL; VZTF01002842; NXB03324.1; -; Genomic_DNA.
DR Proteomes; UP000517678; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; IPR050938; Collagen_Structural_Proteins.
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; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 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:UP000517678};
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..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..456
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..565
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..643
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..694
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..709
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..752
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..769
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..934
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1025
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1044
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXB03324.1"
FT NON_TER 1307
FT /evidence="ECO:0000313|EMBL:NXB03324.1"
SQ SEQUENCE 1307 AA; 136234 MW; 22CA5FFFED7D79A2 CRC64;
TERGSKGHLD LTELIGVPLP PSVYFVTGYG GFPAYSFGAD SNIGRLTSAI IPSPFYRDFA
IVVTVKPNSD RGGVLFAITD AFQKTIYLGL RISPVDDSTQ RIIMYYTEPG SHISREAASF
KVPVMTNRWS RFTVTVEGND VALFMDCEEY QRLQFQRSAR TLVFESGSGI FVGNAGATGL
EKFTGSIQHL TIKSDPRATE DHCEDDDPYA SGDSSGNGSI QEHDVSEPQE ALGSSHLPTR
PEDTLPEPVE APPTILSYLE ENGFSGNHRS EETSEAAKFK EQGTASGFGD SAVMETGQGN
SESTTVTQKM LREEDGSGAG VSPGVSREEV CIMGTEDVEN KDQGPPGSPG KLEQLGQPVS
IFSLLKENMC FRKGSSDPSQ CVKSWSCTAL HTVTSYTSMR WVLAQQLRRI LPAPHACQWP
HRGLGSDNHQ KQRQTAAVPT YRCSRSSNST NSLGSSAVPS QLSGLPGLKG KAGPKGKVGR
EDRLSVKHCI SCQQALQACK CHLTISFLGE TNRFPLYNDP LVSLSKGLPG PPGPPGLPGL
PGKPAPDSGV GPPGSPGEDG ASGEPGPEGP QGPPGRDGVA GPRGWKGEKG DQGLPGSAGP
KGDTGVTGSI GPKGEAGPIG SPGKPGPPGP PGPPGPPGPP GPPGLSYSLG FEDMEGSGSI
DLLSESRIPG SRETKGPKGE KGDPGPQGEP GQDGNSIVGP PGPPGPPGPV IAIPELLLND
TDGIFNFTEI KGLLGPPGPD GKPGLPGFPG PRGPKGDTGL PGSQGPKGQQ GEKGEPGAII
SADGSLTELL GRKGEKGEAG VVGPAGPMGP MGPTGPKGEL GFPGRPGRPG LNGLRGVKGD
RGEAFNGLPG LPGPPGPPGP PGRILYIKGV IFPVPPRPHC KMPVSTPYPG NQEVLNDHGA
KANRDSWGLH SSAHLKGEKG DRGAPGPPGP PLPPSYFSHF INSIKGEKGD NGVTGVKGEK
GEPNGGFFLT GPPGPPGRPG LIGPKGDSVV GPRGPPGLPG LPGLPGYGKI GPPGPPGPPG
PPGPPAIYGS AAAMPGPPGP PGEPGSPATR NLVTTFQNIE GMLEKVHYVA EGTLIYLRET
SEVFIRVRNG WRKLQLGELI PIPADSLPPP AISSHGFQSI PALRPISNMN NGKPALHLVA
LNFPLSGDMR ADFQCFRQAQ LAGLTSTYRA FLSSHLQDLA TVVRKTDRHH LPVVNLQGET
LFSNWESIFD GNGGQFNIHV PIYSFDGRNI MTDSSWPQKV IWHGSTANGI RLVSNYCEAW
HTADTGAMGQ ASPLNTGKLL DQKVYSCNNQ FIVLCIENSF VPDPQRK
//
