ID A0A4X2JTF6_VOMUR Unreviewed; 1204 AA.
AC A0A4X2JTF6;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=MCF.2 cell line derived transforming sequence like {ECO:0008006|Google:ProtNLM};
OS Vombatus ursinus (Common wombat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Vombatidae; Vombatus.
OX NCBI_TaxID=29139 {ECO:0000313|Ensembl:ENSVURP00010000330.1, ECO:0000313|Proteomes:UP000314987};
RN [1] {ECO:0000313|Proteomes:UP000314987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yazar S.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSVURP00010000330.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR STRING; 29139.ENSVURP00010000330; -.
DR Ensembl; ENSVURT00010000382.1; ENSVURP00010000330.1; ENSVURG00010000304.1.
DR Ensembl; ENSVURT00010008478.1; ENSVURP00010007505.1; ENSVURG00010005780.1.
DR GeneTree; ENSGT00940000157874; -.
DR OMA; LQRICTI; -.
DR Proteomes; UP000314987; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd01227; PH_Dbs; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd11857; SH3_DBS; 1.
DR CDD; cd00176; SPEC; 1.
DR Gene3D; 1.20.58.60; -; 1.
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 Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR035534; DBS_PH.
DR InterPro; IPR035532; DBS_SH3.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826:SF115; GUANINE NUCLEOTIDE EXCHANGE FACTOR DBS; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000314987};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 73..245
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 652..832
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 844..966
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1103..1165
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 17..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1204 AA; 136542 MW; A6E53393A6D8C13E CRC64;
MSPVLEESFP LSVSVEKTKK NNNKTLMSQH GSSREGQEGH QYRILRRVSQ ALHGFSSAIL
RPFQKRNWRN NSRHTCSDEI MHQDITPLCA ADIEDQLKKQ FAYLSGGRGQ DGCPVITFPD
YPAFSEIPEK EFQNVLTYLT SIPSLQDTGI GFILVIDRRQ DKWTSVKASV LRIAASFPGN
LQLVLVLRPT GFLQRTLSDI AFKFNRDEFK MKVPIIMLSS VPELQSYIDK TQLTEDLGGT
LDYCHSRWLS HRTAIESFAL MVKQTAQMLQ SFGTELAETE LPNDVQSTSS ILSAHTEKKG
KMKEDMMLAL KEGHTILESI REPLTKNPEY NLNQDQLDNQ TTVQRLLDQL GETEAAFDEF
WVKHQQKLEQ CLQLRNFEQN FREVKAILDV VSERLSTFTD VGNSYAHVEH MLKDLASFEE
KSNEAVEKAR ALSLEGNQLI QSKHYAVDSI LPKCNELQHL CDEFTAEMSR RRNLLQQSLE
LHSLLEKSMK WCDEGIYLLA SQPVDKCQSQ DGAESALQEI EKFLDTGAKN KIQELNKVYK
EYESILNPDL KEHVQKVFQK QESMEEMFQK RQVSLKKLAA KQTRPVQPVA PRPEAFTKSP
CPSPGLRRGS ENSSEGNVAR RGNYRRAKNE MSDIQQGRSG SVMDDEENLA ILRRHVMNEL
IETERAYVEE LLCVLEGYAA EMDNPLMMHL ISSALQNKKD VLFGNMEEIY HFHNRIFLRE
LENYIDYPEL VGRCFLERME DFQIYEKYCQ NKPRSESLWR QCSDCVFFQE CQRKLDHKLS
LDSYLLKPVQ RITKYQLLLK EMLKYSKNCE GAKDLQEALT SILGILKAVN DSMHLIAITG
YDGNLNELGK LLMQGSFSVW TDHKKGHAKV KDLARFKPMQ RHLFLHEKAV LFCKKREENG
EGYEKAPSYS YKQSLNMTAV GITENVKGDI KKFEIWYNAR EEVYIIQAPT PEIKATWVNE
IRKVLTSQLQ ACREASQHRA LEQTQSLPLP TSSNTSPSKN QTKNVKKLEE RKTDPASLEG
YVSSASVQKN PDKSKDASSV VTLTRARWFS SSNLAPASQH RKGWTKTSYS LDAAEDNDGW
SSTEEPLNSS DAEEEGGAGP RKLVPGKYTV VADYDEKGGP EALAVKSGDI VELLHEGEEG
LWFVKNLTTS KEGWVPASNL LALIGNSKSA QSLSSSESGT GSTFLSSSSS CSESCNATFS
DIKG
//
