ECSCR_MOUSE
ID ECSCR_MOUSE Reviewed; 214 AA.
AC Q3TZW0; C3RSF3;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND TISSUE SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204 AND SER-207, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Regulates endothelial chemotaxis and tube formation (By
CC similarity). Has a role in angiogenesis and apoptosis via modulation of
CC the actin cytoskeleton and facilitation of proteasomal degradation of
CC the apoptosis inhibitors BIRC3/IAP1 and BIRC2/IAP2. {ECO:0000250,
CC ECO:0000269|PubMed:19416853}.
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:0000250}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3TZW0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TZW0-2; Sequence=VSP_036454;
CC Name=3;
CC IsoId=Q3TZW0-3; Sequence=VSP_053880;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined, highest
CC expression was observed in lung and spleen endothelial cells.
CC {ECO:0000269|PubMed:19416853}.
CC -!- PTM: May be heavily O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ECSCR family. {ECO:0000305}.
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DR EMBL; EU025067; ABW05063.1; -; mRNA.
DR EMBL; AK157485; BAE34097.1; -; mRNA.
DR EMBL; CX567856; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS37763.1; -. [Q3TZW0-2]
DR CCDS; CCDS89219.1; -. [Q3TZW0-3]
DR RefSeq; NP_001028313.1; NM_001033141.1. [Q3TZW0-2]
DR AlphaFoldDB; Q3TZW0; -.
DR STRING; 10090.ENSMUSP00000095223; -.
DR iPTMnet; Q3TZW0; -.
DR PhosphoSitePlus; Q3TZW0; -.
DR MaxQB; Q3TZW0; -.
DR PRIDE; Q3TZW0; -.
DR ProteomicsDB; 277757; -. [Q3TZW0-1]
DR ProteomicsDB; 277758; -. [Q3TZW0-2]
DR ProteomicsDB; 277759; -. [Q3TZW0-3]
DR Ensembl; ENSMUST00000097618; ENSMUSP00000095223; ENSMUSG00000073599. [Q3TZW0-2]
DR GeneID; 68545; -.
DR KEGG; mmu:68545; -.
DR UCSC; uc008emr.1; mouse. [Q3TZW0-2]
DR CTD; 641700; -.
DR MGI; MGI:1915795; Ecscr.
DR VEuPathDB; HostDB:ENSMUSG00000073599; -.
DR eggNOG; ENOG502S5MK; Eukaryota.
DR GeneTree; ENSGT00400000023549; -.
DR InParanoid; Q3TZW0; -.
DR OrthoDB; 1467702at2759; -.
DR PhylomeDB; Q3TZW0; -.
DR TreeFam; TF351823; -.
DR BioGRID-ORCS; 68545; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ecscr; mouse.
DR PRO; PR:Q3TZW0; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q3TZW0; protein.
DR Bgee; ENSMUSG00000073599; Expressed in right lung lobe and 184 other tissues.
DR ExpressionAtlas; Q3TZW0; baseline and differential.
DR Genevisible; Q3TZW0; MM.
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; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
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; ISO:MGI.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISO:MGI.
DR InterPro; IPR026247; ECSCR.
DR PANTHER; PTHR28602; PTHR28602; 1.
DR Pfam; PF15820; ECSCR; 1.
DR PRINTS; PR02069; ECCREGULATOR.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Apoptosis; Cell membrane; Chemotaxis;
KW Cytoplasm; Developmental protein; Differentiation; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..214
FT /note="Endothelial cell-specific chemotaxis regulator"
FT /id="PRO_0000365018"
FT TOPO_DOM 19..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 23..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..14
FT /note="MRLGSAILGLLLLQ -> MLRDISLEAHGLGSTLTPLLAHQLPQGRVR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036454"
FT VAR_SEQ 1
FT /note="M -> MDREYTEEPATHPADLGTRGAM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19416853"
FT /id="VSP_053880"
SQ SEQUENCE 214 AA; 22689 MW; BFEF3B2FBAFC1D8C CRC64;
MRLGSAILGL LLLQGYSSQP TTTQTSQEIL QKSSQVSLVS NQPVTPRSST MDKQSLSLPD
LMSFQPQKHT LGPGTGTPER SSSSSSSSSS RRGEASLDAT PSPETTSLQT KKMTILLTIL
PTPTSESVLT VAAFGVISFI VILVVVVIIL VSVVSLRFKC RKNKESEDPQ KPGSSGLSES
CSTANGEKDS ITLISMRNIN VNNSKGSMSA EKIL
