ID A0A1S3T6H9_SALSA Unreviewed; 1052 AA.
AC A0A1S3T6H9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Protein ECT2 isoform X2 {ECO:0000313|RefSeq:XP_014072195.1};
GN Name=ect2 {ECO:0000313|RefSeq:XP_014072195.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014072195.1};
RN [1] {ECO:0000313|RefSeq:XP_014072195.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014072195.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014072195.1; XM_014216720.1.
DR AlphaFoldDB; A0A1S3T6H9; -.
DR OrthoDB; 6929at2759; -.
DR Proteomes; UP000087266; Chromosome ssa10.
DR Bgee; ENSSSAG00000070771; Expressed in ovary and 12 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:2000431; P:regulation of cytokinesis, actomyosin contractile ring assembly; IEA:InterPro.
DR CDD; cd17733; BRCT_Ect2_rpt1; 1.
DR CDD; cd17732; BRCT_Ect2_rpt2; 1.
DR CDD; cd01229; PH_Ect2; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 3.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR026817; Ect2.
DR InterPro; IPR049396; ECT2_BRCT0.
DR InterPro; IPR049395; ECT2_PH.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR16777; PROTEIN ECT2; 1.
DR PANTHER; PTHR16777:SF2; PROTEIN ECT2; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF21243; ECT2_BRCT0; 1.
DR Pfam; PF21242; ECT2_PH; 1.
DR Pfam; PF12738; PTCB-BRCT; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00292; BRCT; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF52113; BRCT domain; 2.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 140..212
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 235..323
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 507..696
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 359..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1013
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1052 AA; 118557 MW; 8323A997FD02A7BC CRC64;
MADSSIVTLG MARSLLVDSS VYDSRLAETT KDVFLSLDSE DMEEMLHRVE TRVVLVGEAA
KNGALVKALQ DINMPCIKTD NVKEFGDGEN TEFETVFVLT DFASPDYSYL YKHDNRIVGP
PVVLHCAGRE EPLPFSSRPL YSTTMLNLSL CFTGFRSKEE VKNLVNLVHH MGGAIRKDFS
TKVTHLIAYS THGEKYKLAV CMGTPILTPT WIHKAWEHRD DVKFHAGDEE FRTEFKVPPF
QDCVLSFLGF SDEDKTNMEE RTVKHGGSYL EVGDEKCTHM VVEENSVKEL PFVPSRRLYV
VKQEWFWGSI QMDARAGESM YFYEKMDSPV MKKAVSLLSL NTPNSNRKRR RLRDTLAQLT
KETEISPFPP PRKRPSAEHS LSIGSLLDIS NTPESCKALA ENSVERSRCM RVCAETSRQR
RMRSARERSR GADQEWTFHC SSTPTPQQET GTLEGLPCPQ PAQATEMEEA SWMDSSQESL
YLSAGQEKTE HSRPSKSSTP AVLKQSARWQ VSKELYQTES NYVDILTTVM QLFKLPLEKE
DQVGGPILAQ EEIKTIFGSI PEIYDVHTRI KADLEELVMD WSEDKSVGDI ILKYSKDLVK
AYPPFVNFFE MSKDTIVRCE KQKPRFHAFL KINQSKPECG RQKLVELLIR PVQRLPSVAL
LLNDIKKHTA DENPDRITLE KAIESLKEVM THINEDKRKT EGQKQIFDVV YEVDGCPANL
LSSHRSLVHR VETIALGDKP CDRGENVTLF LFNDCLEIAR KRHKVISTFR SPLGQTRPAA
QLKHITLMPL SQIRRVLDLQ DTEDCHNAFA LVVRPPTEQE NLLFSFQLTT EDTMKSTWLK
MLCRQVANTI CKADAQDLIQ CTEPDSVQVS TKDMDSTLSK ASRVIKKTSK KVTRAFSFTK
TPKRVIQRAF MANSTPDDKS PGPSSENMSR VGSSATLSMA RSTSTFNLSG SAKDSAAAVV
QRSNSLDNAP CPRLRVPVCI HTPDPTPSLP CPEETPPRPQ PTHTMPPYST SPPSLRVPSK
GRIPPGACRY LQVPYSDTRK AGCLSPRKET LL
//
