ID   ECSCR_BOVIN             Reviewed;         197 AA.
AC   Q2KIX5;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Endothelial cell-specific chemotaxis regulator;
DE   AltName: Full=Endothelial cell-specific molecule 2;
DE   Flags: Precursor;
GN   Name=ECSCR; Synonyms=ECSM2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates endothelial chemotaxis and tube formation. Has a
CC       role in angiogenesis and apoptosis via modulation of the actin
CC       cytoskeleton and facilitation of proteasomal degradation of the
CC       apoptosis inhibitors BIRC3/IAP1 and BIRC2/IAP2 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with FLNA. Interacts with the 20S proteasome subunit
CC       PSMA7. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250}.
CC   -!- PTM: May be heavily O-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ECSCR family. {ECO:0000305}.
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DR   EMBL; BC112471; AAI12472.1; -; mRNA.
DR   RefSeq; NP_001039564.1; NM_001046099.2.
DR   RefSeq; NP_001231374.1; NM_001244445.1.
DR   RefSeq; NP_001231375.1; NM_001244446.1.
DR   AlphaFoldDB; Q2KIX5; -.
DR   SMR; Q2KIX5; -.
DR   STRING; 9913.ENSBTAP00000040657; -.
DR   PaxDb; Q2KIX5; -.
DR   GeneID; 511765; -.
DR   KEGG; bta:511765; -.
DR   CTD; 641700; -.
DR   eggNOG; ENOG502S5MK; Eukaryota.
DR   HOGENOM; CLU_101826_1_0_1; -.
DR   InParanoid; Q2KIX5; -.
DR   OrthoDB; 1467702at2759; -.
DR   TreeFam; TF351823; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IBA:GO_Central.
DR   GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IBA:GO_Central.
DR   GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IBA:GO_Central.
DR   InterPro; IPR026247; ECSCR.
DR   PANTHER; PTHR28602; PTHR28602; 1.
DR   Pfam; PF15820; ECSCR; 1.
DR   PRINTS; PR02069; ECCREGULATOR.
PE   2: Evidence at transcript level;
KW   Angiogenesis; Apoptosis; Cell membrane; Chemotaxis; Cytoplasm;
KW   Developmental protein; Differentiation; Glycoprotein; Membrane;
KW   Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..197
FT                   /note="Endothelial cell-specific chemotaxis regulator"
FT                   /id="PRO_0000365015"
FT   TOPO_DOM        24..113
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..197
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          40..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TZW0"
SQ   SEQUENCE   197 AA;  20639 MW;  5B846874402B3BA2 CRC64;
     MGSVRETQLR WAILGFLLLQ AASETPSQFS TEAMTLSSST VADHLPSSPG PTWSQSQKHT
     SGLSADVPSS GRSSDSMSGD TSHNVTSTSP NMSFRTTADS TVPPSPTSET VLTVAAFGVI
     SFIAILVVVV IVLVSVVSLR FKCRKNKESE DPQKPGSSGL SESGSTANGE KESITLISMK
     NINMNNSKGC PSAEKVL