ID A0A3B5QXV2_XIPMA Unreviewed; 966 AA.
AC A0A3B5QXV2;
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=Rho/Rac guanine nucleotide exchange factor 2 {ECO:0000313|Ensembl:ENSXMAP00000035176.1};
GN Name=ARHGEF2 {ECO:0000313|Ensembl:ENSXMAP00000035176.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000035176.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000035176.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000035176.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR AlphaFoldDB; A0A3B5QXV2; -.
DR STRING; 8083.ENSXMAP00000035176; -.
DR Ensembl; ENSXMAT00000028096.1; ENSXMAP00000035176.1; ENSXMAG00000017818.2.
DR GeneTree; ENSGT00940000158341; -.
DR InParanoid; A0A3B5QXV2; -.
DR OMA; SECITEA; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 3.30.60.20; -; 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; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR13944; AGAP007712-PA; 1.
DR PANTHER; PTHR13944:SF20; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 40..87
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 235..432
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 472..572
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 107704 MW; 47F1B51CB1B7EA48 CRC64;
MSRLLESRRE KDRMKESSLK IKEKERLKET REREARSSSG HLFTSLSVSA TTLCSSCNKS
ITAKEALSCP GCNVTIHNRC RDSVASCAKM KQRQQKLTLV RNNSALQNVA LRTKTPMMKE
RPSSAIYPSD TLRQSLLGSR RVRTGLTLAK SVSTNNIAGG TEESVGLRRI LSQSTESLNF
RNRTLSMESL TDDGEWWWSP LLEELQEEGG CVQADSWSMA VDSKFLQMQH KDVIKQQDVI
YELIQTEFHH VRTLRIMEGV YRRGMQEEVL LEAGVVHTIF PCLDQLLELH TNFLSQLLSR
RKDGLQEGSA NNFTVRRLGD LLLRQFSGQC AEDMKKLYSE FCSRHPKAVK LYKEVLNRDR
RLQQFIRRVC RGPLLRRHGV QECILLVTQR ITKYPVLIQR ILDNTKGCPD ERRDLQEALV
LLKELIGSVD QEVLELDRNR RLQEVQARLD PRAQAEVKGG GAFRGGELLR RKLLHEGTLT
WKVQGSRMKD VQVLLMSDIL VFLQEKDQKF TFASLDKSPV VSLTKLIVRE VANQEKGMYL
ISDSAPPEMY ELYASSKDDR KTWMSCIQKA AQSCPSRDEF PLIETEDKAL QRRLRADIQQ
KDKEVLELLQ ERATLFSDLV QATAREDGEE RRVEAKTSSC NRNLFRADTP HAPKAEPLLL
AAIGEVDKLA ALLSDTSNQK SSVTNGNQDI SRPERKPAAG TDPERGSAPA AGRAQHAASR
PAGGGDPAGL DPGAVGGRRP PGWPWLRPPP SAVDVARCGA GRQWRGGAAA PAGGAAAGGA
VAAASEGGRG WQEGGGLRKE EKEEQREGRR LQGPAGASGE PGDVATANSA EVRCFSQQVD
RKPEAEPPAV APLALEDPVD QLDGLEEGLE EEEDEEVMKI SPRSDSPRGQ YRRHCRAPHC
HHGNRRSVTP QTSRTFPRRA RANLPVDVAA MMSPSLPEIH SLSDIFLQHF LNFLFDTGSV
TMTTVY
//
