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Database: UniProt
Entry: A0A3B4VA99_SERDU
LinkDB: A0A3B4VA99_SERDU
Original site: A0A3B4VA99_SERDU 
ID   A0A3B4VA99_SERDU        Unreviewed;      1043 AA.
AC   A0A3B4VA99;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=MCF.2 cell line derived transforming sequence {ECO:0000313|Ensembl:ENSSDUP00000026870.1};
GN   Name=MCF2 {ECO:0000313|Ensembl:ENSSDUP00000026870.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000026870.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000026870.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3B4VA99; -.
DR   STRING; 41447.ENSSDUP00000026870; -.
DR   Ensembl; ENSSDUT00000027347.1; ENSSDUP00000026870.1; ENSSDUG00000019428.1.
DR   GeneTree; ENSGT00940000156974; -.
DR   OMA; HNRRWPG; -.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd11857; SH3_DBS; 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   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR035899; DBL_dom_sf.
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   PANTHER; PTHR22826:SF146; PROTO-ONCOGENE DBL; 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   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SMART; SM00150; SPEC; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 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   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..160
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   DOMAIN          568..747
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          765..881
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          959..1020
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          888..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        888..913
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1043 AA;  118450 MW;  7E5642F14B8E709A CRC64;
     VTVPVSMKEV GGYIEKQVAY LSGRGEDSSV IITLPECSAF SDIPEEALAK VFTYLTLIPT
     RQPGVKFIII LDRRLDTWAS IKTALARIAA SFPGNLHLVL VLRPTSFFHR TVTDIGFRFS
     QEDFMLKMPV VMLSSVTDLL RYISENQLTS EFGGTLDYCH SDWIVLRTAI ESFAVTVKDI
     AHMLQGFGTD LAETELPDKG KAIEYLLECQ TDKYRKLKDA IRSVSKEGRH LLSSLETSGK
     EDDSQWDVKL DWETVQLLAQ LRDMESAFDG FFEKHHLKLH QYMQLLRYEQ SFQEMELCLE
     HLMAQERALS ISVDTLAQTE QALKRLDSLE SNAQEVVARA QIIILHGHQL SASHHYAIAL
     IMQRCNELRH YCDTLNAALK TKHSRLLHTH QLLLCLGQAQ TWCDDGAYML ANQLVERFQS
     KEGAQAALRD IEKFLEGAPS VLSSGPEILA IEYEAVITPQ LQAHIGKTFE KHAAVQQMIQ
     NRQTCLKKLA DKHVRPIQLV APRPENPPRS KSPLFSPKHL KFTFDISLPG KRASRKSPNP
     RKIEVIHDYQ ESRSCVSYGL EGEDSPDLLK HVMRELVETE RIYVEELLSV LLGYRAEMDN
     PALWGLLPPI LRSKRDILFG NMPEIYNFHS VFLQDLEGCL EAPEGVGACF LERKESFQIY
     ECYCQNKPRS EALLRQFSDC AFFLECQKKL EHKLGLESYL LKPVQRLTKY QLLLKELLKY
     STDCEGTSEL QGALTAMLDL LKSVNDSMHQ IAITGYEGDI CELGRVLMQG SFSVWISHKK
     GPTRMKELAR FKPMQRHLFL YERALLFCKR REEHGDGSDK TPSYSFKHCL KMTAVGITEN
     VKGDVKKFEI WYSGREEVYV VQAPTLEVKM AWLNELRRIL TNQQKLLRSK QQRASVSSED
     TESGRSSPDP QPHSPKHQHN RRWPGAHHSV DICEGLEEWS GGRDAFHPSD TEEEVLVQLA
     PGRYRALADC LQNGPDSITI KCGDVIQLQC EDNKGRRLVK NLSRRQEGFI AAASLQLIIG
     DSSRGHSSRL GPGNLKARKL SSP
//
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