ID A0A7K6BZM5_PTIVI Unreviewed; 1330 AA.
AC A0A7K6BZM5;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 08-OCT-2025, entry version 17.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
DE Flags: Fragment;
GN Name=Col15a1_1 {ECO:0000313|EMBL:NWV06920.1};
GN ORFNames=PTIVIO_R09764 {ECO:0000313|EMBL:NWV06920.1};
OS Ptilonorhynchus violaceus (Satin bowerbird) (Pyrrhocorax violaceus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Ptilonorhynchidae; Ptilonorhynchus.
OX NCBI_TaxID=28724 {ECO:0000313|EMBL:NWV06920.1, ECO:0000313|Proteomes:UP000584880};
RN [1] {ECO:0000313|EMBL:NWV06920.1, ECO:0000313|Proteomes:UP000584880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-012-10 {ECO:0000313|EMBL:NWV06920.1};
RC TISSUE=Blood {ECO:0000313|EMBL:NWV06920.1};
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:NWV06920.1}.
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DR EMBL; VZRJ01005051; NWV06920.1; -; Genomic_DNA.
DR Proteomes; UP000584880; 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 2.
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:UP000584880};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 7..195
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 56..194
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 192..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..567
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..588
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..666
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..717
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..732
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..775
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..792
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..945
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..957
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1048
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1067
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWV06920.1"
FT NON_TER 1330
FT /evidence="ECO:0000313|EMBL:NWV06920.1"
SQ SEQUENCE 1330 AA; 139892 MW; 980CD3ED2DCCE986 CRC64;
ERGSKGHLDL TELIGVPLPP SVYFVTGYGG FPAYSFAPDS NIGRLTSAII PSPFYRDFAI
VVTVKPSSDR GGVLFAITDA FQKTIYLGLR ISPVDDSTQR IIMYYTEPGS HISREAASFK
VPVMTNRWNR FTVTVQGNDV ALFMDCEEYQ RLRFQRSART LVFESGSGIF VGNAGATGLE
KFTGSIQHLT IKSDPRATED HCEDDDPYAS GDSSGNGSIQ EHDVSEAQEA LAPSHIPIRP
EDTLAEPVEA PPTILSYLEE NDFSGNHRSE ETSEAAKLKE QGTALGSAVM ETGQGNSEST
TVTENILREE DGSGVGVLPE LNREETPSGA KQSVSLTLHR HMLPYCLLLT SAAINFVVES
IFELIECTSH PLTLCSNLTT LCPSFLLSFL CIPLLYPLVS HLLSGSWGIP SHLLQVTPSL
TIKLRNLLIE YHGVTTLTTY XAYITYPENA RSTVKPYSGK TNALCNAVNA ACTFANSLQK
LEKEEFLLPL PMQRSYFLEA CPRNGLSPTL HLSSHSCDWK YTQIAASAYN VYMVKSLLMY
LNSHFRVILG LPGPPGPPGL PGLPGKPAPD SGVGPPGSPG EDGASGEPGP EGPQGPPGRD
GVVGPQGWKG EKGDQGLPGS AGPKGDTGVT GSIGPKGEAG PVGSPGKPGP PGPPGPPGPP
GPPGPPGLSY SLGFEQGKVH LVIFPVKSRM LISFYHLQGP KGEKGDPGPQ GEPGQDGNSI
VGPPGPPGPP GPVIAIPELL LNDTDGILNF TEIKGLLGPP GPDGKPGLPG FPGPRGPKGD
TGLPGLQGPK GQQGEKGEPG AIISADGTLT ELLGRKGEKG EAGVMGPAGP MGPIGPTGPK
GELGFPGRPG RPGLNGLRGV KGDRGEAFNG LPGLPGPPGP PGPPGRILYI KGVIFPVPPR
PHCKMPVSTP YPGNQEALND HGAKANRDSW GLHRSADLKG EKGDRGAPGP PGPPLPPSYF
SHFINSIKGE KGDNGVTGVK GEKGEPNGGF FLTGPPGPPG RPGLIGPKGD SVVGPRGPPG
LPGLPGLPGY GKIGPPGPPG PPGPPGPPAI YGSAAAMPGP PGPPGEPGSP ATRNLVTTFQ
NIEGMLEKVH YVAEGTLIYL RETSEVFIRV RNGWRKLQLG ELIPIPADSL PPPAISSHGF
QPIPALRPIS NMNNGKPALH LVALNFPLSG DMRADFQCFR QAQLAGLTST YRAFLSSHLQ
DLATVVRKTD RYHLPIVNLQ GETLFSNWES IFDGNGGQFN VHVPIYSFDG RNIMTDSSWP
QKVIWHGSTA NGIRLVSNYC EAWHTADMGA MGQASPLKTG KLLDQKVYSC NNQFIVLCIE
NSFVSDPQGK
//
