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Database: UniProt
Entry: A0A3B4EHD2_PYGNA
LinkDB: A0A3B4EHD2_PYGNA
Original site: A0A3B4EHD2_PYGNA 
ID   A0A3B4EHD2_PYGNA        Unreviewed;      1166 AA.
AC   A0A3B4EHD2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=MCF.2 cell line derived transforming sequence like {ECO:0000313|Ensembl:ENSPNAP00000035158.1};
GN   Name=MCF2L {ECO:0000313|Ensembl:ENSPNAP00000035158.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000035158.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000035158.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3B4EHD2; -.
DR   Ensembl; ENSPNAT00000027774.1; ENSPNAP00000035158.1; ENSPNAG00000025029.1.
DR   GeneTree; ENSGT00940000157874; -.
DR   Proteomes; UP000261440; 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; cd01227; PH_Dbs; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd00170; SEC14; 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   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
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   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   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SMART; SM00326; SH3; 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   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..173
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   DOMAIN          571..751
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          769..885
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1068..1129
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          507..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          917..954
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          974..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1040..1069
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1132..1166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..544
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1002
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1054
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1166 AA;  130954 MW;  5113C20EBB7AC4C1 CRC64;
     MPLVTNEIMQ QESSPLCAAD IGPDLSKGFA FLSGGRGENG SPIIIFPEFP AFSELQEQEF
     HNVLTYLTSV PSLSASGVGF ILVIDRRQDR WASVKGTLLR IAGSFPGNLQ LVLVLRPTTL
     LQRTLSDFLF KFSKDEFKMK VPVIMLSSVT ELHSYIDRTQ LTQELGGTQE YCHEKWISHR
     TAIEGFALMV KKTAQTLQAF GTELAETELP NDVEATSNLL TTHTEKKDKM KEDLKIALSQ
     GGRLLESINE PFVSNPDYNM NHDELENLAT VQRLLGQLDE TETAFDDFWE RHQTKLEQCL
     QLRHFEHNFR EVRAHLDQVA DKLSGFSEVG ISPAHGEHIL KELTNHEERT CEVLDRALAL
     ASDADILIES SHYAVDSILP KCSELRAVCE EVGTVLKAKK AHLLKAMELH SSLEKATKWC
     EDGIYLLASQ PVDKCQSQDG AEAALQEIER YLDTANQHKL TDLNGIWRDY ESVLTSDFRE
     QVERVFQKQL SMQEMFEKRR ISLKKLAAKQ TRPVQPVAPR PEAIIKSPHS SPAHREKDSS
     PDINNKKGDA LIQNGSRPPS LSEEEENLAV LRRHVMNELL ETERAYVEEL LCVLQGYADE
     MDNPSMAHLI PITLHNKKDV LFGNMAEIYQ FHNKTFLREL EAYTDYPELV GRCFLERMTD
     LQIYEKYCQN KPRSESLWRQ CSDCAFFQEC QKKLEHKLGL DSYLLKPVQR ITKYQLLLKE
     LLKYSKGCEG SEDLQDALSS ILGILKAVND SMHLIAITGY EGNLSELGRL LMQGSFSVWT
     EHKKGHAKVK DLARFKPMQR HLFLHEKALL FCKKREENGE GYEKAPSYSF KHSLSMSAVG
     ITENAKGDNK KFEIWCNSRE EVYIVQAPTT EIKTAWVNEI RKVLTGQLKA CREASQQKTS
     EQVSPLPNAV ISLSPFKTNQ KTVKKGEEKK VETTVPDSGL APSSKNTDKI KDEAVISPSA
     DRAAVAKKRF TLQGFSNLKS QKGSPPSPDH KTKRHEIKSD PTPFGFRDAG PHVTLSRVKW
     LSTSSLLQAK RRGFNKASLS MDASEENDGY SSAEDPLNSD PEDEGKKLSP GRYVVVADYD
     KGGAQDLSVK SGDMVQLVRE GSDGQWFVRN LKNSKEGWMP AANLLTLIGE SKSSQSLTSS
     EGSGSGNLST SSSCSETYTS FSDIKP
//
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