ID   A0A2K6GD09_PROCO        Unreviewed;       704 AA.
AC   A0A2K6GD09;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=BMP binding endothelial regulator {ECO:0000313|Ensembl:ENSPCOP00000024109.1};
GN   Name=BMPER {ECO:0000313|Ensembl:ENSPCOP00000024109.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000024109.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000024109.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A2K6GD09; -.
DR   STRING; 379532.ENSPCOP00000024109; -.
DR   Ensembl; ENSPCOT00000034789.1; ENSPCOP00000024109.1; ENSPCOG00000024214.1.
DR   GeneTree; ENSGT00940000156485; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0002043; P:blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0042118; P:endothelial cell activation; IEA:Ensembl.
DR   GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IEA:Ensembl.
DR   GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0010594; P:regulation of endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
DR   GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR   CDD; cd19941; TIL; 1.
DR   Gene3D; 6.20.200.20; -; 4.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   InterPro; IPR036084; Ser_inhib-like_sf.
DR   InterPro; IPR002919; TIL_dom.
DR   InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom.
DR   InterPro; IPR001007; VWF_dom.
DR   InterPro; IPR001846; VWF_type-D.
DR   PANTHER; PTHR46698; CROSSVEINLESS 2; 1.
DR   PANTHER; PTHR46698:SF4; CROSSVEINLESS 2; 1.
DR   Pfam; PF08742; C8; 1.
DR   Pfam; PF01826; TIL; 1.
DR   Pfam; PF00093; VWC; 2.
DR   Pfam; PF00094; VWD; 1.
DR   SMART; SM00832; C8; 1.
DR   SMART; SM00214; VWC; 4.
DR   SMART; SM00216; VWD; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 4.
DR   SUPFAM; SSF57567; Serine protease inhibitors; 1.
DR   PROSITE; PS01208; VWFC_1; 2.
DR   PROSITE; PS50184; VWFC_2; 2.
DR   PROSITE; PS51233; VWFD; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           40..704
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014333707"
FT   DOMAIN          183..244
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          318..377
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          381..554
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
SQ   SEQUENCE   704 AA;  78131 MW;  2A3FE5FB78A65E35 CRC64;
     MLWFSGVRAL AERPCRRSPG ITCCVLLLLN CSGVPMSLAS SFLTGSVAKC ENEGEVLQIP
     FITDNPCIMC VCSLCVRILG VLFDACFKCV LSLFEVTCKR EKCPVLSRDC ALAVKQRGAC
     CERCKGCTYE GNTYNSSFKW QSPAEPCVLR QCQEGVVTES EVRCVVHCKN PLEHLGSCCP
     ACPGCVFEGV QYREGEEFQP EGSKCTKCSC AGGRTQCVRE VCPILSCPQH LSHIPPGQCC
     PKCLGQRKVF DLPFGSCLFR SDVYDNGSSF LYDNCTTCTC RDSTVICKKK CSRPGSCNKG
     GEGCCEECLL RVPPEDIKMC KFGNKIFRDG EMWSSVNCTI CACVKGRTEC RKKQCIPISS
     CPQGKILNRK GCCPICTEKP GVCTVFGDPH YNTFDGRTFN FQGTCQYVLT KDCSSPASPF
     QVLVKNDARR TRSFSWTKSV ELVLGESRVS LQQHLTVRWN GTRIALPCHA PHFHADLDGY
     LLKVTTKAGL EISWDGDSFV EVMAAPYLKG KLCGLCGNYN GHKRDDLIGG DGNFKFDVDD
     FAESWRVESN EFCNRPQRKP VPELCQGTVK VKLRAHRECQ KLKSWEFQTC HSTVDYATFY
     RSCVTDMCEC PVHKNCYCES FLAYTRACQR EGIKVHWEPQ QNCAATQCKH GAVYDTCGPG
     CVKTCDNWNE IGPCNKPCVA GCHCPANLVL HKGRCIKPVL CPQR
//