ECSCR_CANLF
ID ECSCR_CANLF Reviewed; 175 AA.
AC P0C8R9;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 52.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Staten N.R.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 49-175 (ISOFORM 1).
RC TISSUE=Heart ventricle;
RA Balija V.S., Nascimento L.U., McCombie W.R.;
RT "ESTs from Canis familiaris left cardiac ventricle (dog).";
RL Submitted (DEC-2004) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0C8R9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0C8R9-2; Sequence=VSP_036453;
CC -!- PTM: May be heavily O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ECSCR family. {ECO:0000305}.
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DR EMBL; DN443643; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AAEX02023193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CX001226; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0C8R9; -.
DR SMR; P0C8R9; -.
DR STRING; 9612.ENSCAFP00000031760; -.
DR Ensembl; ENSCAFT00030006718; ENSCAFP00030005900; ENSCAFG00030003567. [P0C8R9-2]
DR Ensembl; ENSCAFT00040005766; ENSCAFP00040004966; ENSCAFG00040003008. [P0C8R9-2]
DR Ensembl; ENSCAFT00845001581; ENSCAFP00845001251; ENSCAFG00845000875. [P0C8R9-2]
DR eggNOG; ENOG502S5MK; Eukaryota.
DR GeneTree; ENSGT00390000008582; -.
DR HOGENOM; CLU_101826_1_0_1; -.
DR InParanoid; P0C8R9; -.
DR TreeFam; TF351823; -.
DR Proteomes; UP000002254; Chromosome 2.
DR Bgee; ENSCAFG00000023602; Expressed in bone marrow and 50 other tissues.
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; 2.
DR Pfam; PF15820; ECSCR; 1.
DR PRINTS; PR02069; ECCREGULATOR.
PE 2: Evidence at transcript 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..175
FT /note="Endothelial cell-specific chemotaxis regulator"
FT /id="PRO_0000365016"
FT TOPO_DOM 25..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 33..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TZW0"
FT VAR_SEQ 58..95
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036453"
FT CONFLICT 139
FT /note="S -> F (in Ref. 3; CX001226)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="I -> L (in Ref. 1; DN443643 and 3; CX001226)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 175 AA; 18248 MW; D65595F9B1E1B0C0 CRC64;
MGTVRAARLC GAILGFLLLQ GAFGKPSLIT EPLSSNTGNS SSSEPRSSSS PASAGTPDTS
QNITPISTTM SLRIREDSTI LPSPTSETVL TVAAFGVISF IVILVVVVII LVSVVSLRFK
CRKNKESEDP QKPGSSGLSE SCSTANGEKD SITLISMKNI NMNNSKGCPT AEKVI
