ECSCR_HUMAN
ID ECSCR_HUMAN Reviewed; 205 AA.
AC Q19T08; B4E3H7; C3RSF2;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Endothelial cell-specific chemotaxis regulator;
DE AltName: Full=Apoptosis regulator through modulating IAP expression;
DE Short=ARIA;
DE AltName: Full=Endothelial cell-specific molecule 2;
DE Flags: Precursor;
GN Name=ECSCR; Synonyms=ECSM2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GLYCOSYLATION, INTERACTION WITH FLNA,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=18556573; DOI=10.1161/atvbaha.108.162511;
RA Armstrong L.-J., Heath V.L., Sanderson S., Kaur S., Beesley J.F.J.,
RA Herbert J.M.J., Legg J.A., Poulsom R., Bicknell R.;
RT "ECSM2, an endothelial specific filamin a binding protein that mediates
RT chemotaxis.";
RL Arterioscler. Thromb. Vasc. Biol. 28:1640-1646(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH PSMA7.
RX PubMed=19416853; DOI=10.1073/pnas.0806780106;
RA Ikeda K., Nakano R., Uraoka M., Nakagawa Y., Koide M., Katsume A.,
RA Minamino K., Yamada E., Yamada H., Quertermous T., Matsubara H.;
RT "Identification of ARIA regulating endothelial apoptosis and angiogenesis
RT by modulating proteasomal degradation of cIAP-1 and cIAP-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8227-8232(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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.
CC {ECO:0000269|PubMed:18556573, ECO:0000269|PubMed:19416853}.
CC -!- SUBUNIT: Interacts with FLNA. Interacts with the 20S proteasome subunit
CC PSMA7. {ECO:0000269|PubMed:18556573, ECO:0000269|PubMed:19416853}.
CC -!- INTERACTION:
CC Q19T08; O14818: PSMA7; NbExp=3; IntAct=EBI-15778214, EBI-603272;
CC Q19T08; P60484-1: PTEN; NbExp=4; IntAct=EBI-15778214, EBI-15722967;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cytoplasm.
CC -!- TISSUE SPECIFICITY: Highest expression in endothelial cells. Also
CC detected in vascular smooth muscle, macrophages, lymphocytes, and mast
CC cells. {ECO:0000269|PubMed:18556573, ECO:0000269|PubMed:19416853}.
CC -!- PTM: May be heavily O-glycosylated. {ECO:0000269|PubMed:18556573}.
CC -!- SIMILARITY: Belongs to the ECSCR family. {ECO:0000305}.
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DR EMBL; DQ462572; ABE73209.1; -; mRNA.
DR EMBL; EU025066; ABW05062.1; -; mRNA.
DR EMBL; AK304726; BAG65489.1; -; mRNA.
DR EMBL; BC146912; AAI46913.1; -; mRNA.
DR EMBL; BC146913; AAI46914.1; -; mRNA.
DR CCDS; CCDS75317.1; -.
DR RefSeq; NP_001071161.1; NM_001077693.3.
DR RefSeq; NP_001280668.1; NM_001293739.1.
DR AlphaFoldDB; Q19T08; -.
DR BioGRID; 567392; 33.
DR DIP; DIP-60344N; -.
DR IntAct; Q19T08; 5.
DR STRING; 9606.ENSP00000479243; -.
DR GlyGen; Q19T08; 3 sites, 3 O-linked glycans (3 sites).
DR iPTMnet; Q19T08; -.
DR PhosphoSitePlus; Q19T08; -.
DR BioMuta; ECSCR; -.
DR DMDM; 121940639; -.
DR jPOST; Q19T08; -.
DR MassIVE; Q19T08; -.
DR PaxDb; Q19T08; -.
DR PeptideAtlas; Q19T08; -.
DR PRIDE; Q19T08; -.
DR ProteomicsDB; 61198; -.
DR Antibodypedia; 66705; 94 antibodies from 16 providers.
DR DNASU; 641700; -.
DR Ensembl; ENST00000618155.3; ENSP00000479243.1; ENSG00000249751.4.
DR Ensembl; ENST00000673382.1; ENSP00000500743.1; ENSG00000288297.1.
DR GeneID; 641700; -.
DR KEGG; hsa:641700; -.
DR MANE-Select; ENST00000618155.3; ENSP00000479243.1; NM_001077693.4; NP_001071161.1.
DR UCSC; uc032vne.2; human.
DR CTD; 641700; -.
DR DisGeNET; 641700; -.
DR GeneCards; ECSCR; -.
DR HGNC; HGNC:35454; ECSCR.
DR HPA; ENSG00000249751; Low tissue specificity.
DR neXtProt; NX_Q19T08; -.
DR OpenTargets; ENSG00000249751; -.
DR PharmGKB; PA164718891; -.
DR VEuPathDB; HostDB:ENSG00000249751; -.
DR eggNOG; ENOG502S5MK; Eukaryota.
DR GeneTree; ENSGT00400000023549; -.
DR HOGENOM; CLU_101826_1_0_1; -.
DR InParanoid; Q19T08; -.
DR OMA; FKCQKSK; -.
DR OrthoDB; 1467702at2759; -.
DR PhylomeDB; Q19T08; -.
DR PathwayCommons; Q19T08; -.
DR SignaLink; Q19T08; -.
DR BioGRID-ORCS; 641700; 3 hits in 238 CRISPR screens.
DR ChiTaRS; ECSCR; human.
DR GenomeRNAi; 641700; -.
DR Pharos; Q19T08; Tbio.
DR PRO; PR:Q19T08; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q19T08; protein.
DR Bgee; ENSG00000249751; Expressed in upper lobe of left lung and 93 other tissues.
DR Genevisible; Q19T08; HS.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; IMP:MGI.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IMP:MGI.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IMP:MGI.
DR InterPro; IPR026247; ECSCR.
DR PANTHER; PTHR28602; PTHR28602; 2.
DR Pfam; PF15820; ECSCR; 1.
DR PRINTS; PR02069; ECCREGULATOR.
PE 1: Evidence at protein 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..205
FT /note="Endothelial cell-specific chemotaxis regulator"
FT /id="PRO_0000365017"
FT TOPO_DOM 25..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 49..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TZW0"
FT CONFLICT 69
FT /note="T -> I (in Ref. 3; BAG65489)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 205 AA; 21295 MW; 7CB22DEF4B6ADCAD CRC64;
MGTAGAMQLC WVILGFLLFR GHNSQPTMTQ TSSSQGGLGG LSLTTEPVSS NPGYIPSSEA
NRPSHLSSTG TPGAGVPSSG RDGGTSRDTF QTVPPNSTTM SLSMREDATI LPSPTSETVL
TVAAFGVISF IVILVVVVII LVGVVSLRFK CRKSKESEDP QKPGSSGLSE SCSTANGEKD
SITLISMKNI NMNNGKQSLS AEKVL
