ID A0A2D0S258_ICTPU Unreviewed; 1148 AA.
AC A0A2D0S258;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Rho guanine nucleotide exchange factor 2 {ECO:0000256|ARBA:ARBA00017262};
DE AltName: Full=Guanine nucleotide exchange factor H1 {ECO:0000256|ARBA:ARBA00031760};
GN Name=arhgef1a {ECO:0000313|RefSeq:XP_017336838.1,
GN ECO:0000313|RefSeq:XP_017336839.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017336839.1};
RN [1] {ECO:0000313|RefSeq:XP_017336838.1, ECO:0000313|RefSeq:XP_017336839.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017336838.1,
RC ECO:0000313|RefSeq:XP_017336839.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186}. Cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00004541}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}.
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DR RefSeq; XP_017336838.1; XM_017481349.3.
DR RefSeq; XP_017336839.1; XM_017481350.3.
DR STRING; 7998.ENSIPUP00000015424; -.
DR Ensembl; ENSIPUT00000016081; ENSIPUP00000015424; ENSIPUG00000010417.
DR GeneID; 108272707; -.
DR KEGG; ipu:108272707; -.
DR CTD; 368266; -.
DR OrthoDB; 2917157at2759; -.
DR Proteomes; UP000221080; Chromosome 12.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; 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:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR CDD; cd20877; C1_ARHGEF2; 1.
DR CDD; cd13393; PH_ARHGEF2; 1.
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; IPR037806; ARHGEF2_PH.
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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell junction {ECO:0000256|ARBA:ARBA00022427};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 266..313
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 463..660
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 700..801
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1010..1054
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 23..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1148 AA; 128544 MW; 1C396E301E45B31E CRC64;
MGPEEQPHLK DTMSNTPLSS PHPHGCSPAP SAPLPSPPIS PARTGVVTFR SPATRHLAHL
DAWRRHSWEP GAALQGNPAS DTRSVSLEDL DMEEMALVLG GALGCHRARD TRRSVTCEGS
LSSLTEEEAG IETQSQLCST LEEQASQMYS CSVSAPSLCV VRRTAKASAP RPRSYCYDNN
AENSLYYQGG GSTQSLDREL SSLHWEAGRE TKGESDEDKE EVAGNAFVRT FSFLYKMTSS
RKNKEKERMR EREREARERE ARYTNGHLFT SLTVSGTTLC SACNKSITAK EALSCPTCNV
TIHNRCRDSL PNCAKMKQRQ QKLALMRNSS SYSGTVTLRN KTHLKERPSS AIYPSDSLRQ
SLLGSRRGRS SLLLSKSVST NNIAGTLSDD SPLGLRRILS QSTDSLNFRS RTMSMESLND
EGEVYYASVL EELEIEGRDF EADSWSMVVD SAYLQTHRKD IIKRQDVIYE LIQTELHHVR
TLRIMDGVFR RGMLDEVQLE PGVVHALFPC LEKLLVLHTR FLTQLLNRRL HCLQPDSTHN
FTISRISDLL MQQFSGQCAD EMKKTYAEFC SGHLKAVKLY KELLARDKRL QYFIRKVSRG
PLLRRHGFQE CILLVTQRIT KYPVLVQRIL DNTKDNPEEE VGLKQALTLL RDLLNGVEQQ
VLELERTQRL QEIRSRLDPR SQAKMRSDAM FRPAELLRRQ LIHEGTLLWK TPSSRLKDVQ
VLLMTDVLVF LQEKDQRYIF ASLDKSAVVS LQNLLVRDIA NQERGLFLIS SEFSPPEMYE
LHAASKDDRN TWIRHIQQAV SRCPSREEFP LIETEDKALL RRLKADIQQK DREVLELLQE
RVTLFSDLAE VMCGQELVLP PNSRNLFRAD TPQAPRGEQL LTQAITEVDR LTELLLGSGS
GIPLACTING HHNCTGALLI NGQEVLVNGS QETAASQDGN GNQLEDKTPS EEVSQRLVNL
SAQLHALQGA VIRQDSIVEF CAREGGTSRS RPGRSLSREG TGEVGTAGEL ALLQRQHSLL
QEELVRLRGA EGRLKDSEKA RAQLEKQLRG LKSNSAALGE STGHAQALLH RKGSETDPNT
DTPLASQASM EQTDGQQDGS DIDVDVISDD DDDEDLKVSP RSESPRDLQD IPEESESSAE
AREHASHC
//
