ID H3AF10_LATCH Unreviewed; 1027 AA.
AC H3AF10;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=ARHGEF2 {ECO:0000313|Ensembl:ENSLACP00000008231.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000008231.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000008231.1}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AFYH01158037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01158038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01158039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01158040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01158041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01158042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01158043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01158044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01158045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01158046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006005168.1; XM_006005106.2.
DR AlphaFoldDB; H3AF10; -.
DR STRING; 7897.ENSLACP00000008231; -.
DR Ensembl; ENSLACT00000008297.1; ENSLACP00000008231.1; ENSLACG00000007285.1.
DR GeneID; 102363693; -.
DR KEGG; lcm:102363693; -.
DR CTD; 9181; -.
DR eggNOG; KOG3520; Eukaryota.
DR GeneTree; ENSGT00940000158341; -.
DR HOGENOM; CLU_002466_1_1_1; -.
DR InParanoid; H3AF10; -.
DR OMA; RVFQQGM; -.
DR OrthoDB; 2917157at2759; -.
DR TreeFam; TF325887; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000007285; Expressed in pelvic fin and 6 other cell types or tissues.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
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; IPR036263; Chorismate_II_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; 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; SSF48600; Chorismate mutase II; 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 Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 79..126
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 277..474
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 514..614
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 726..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 633..667
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 731..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1027 AA; 117480 MW; BAAFC0C2170EA3B9 CRC64;
MRLLHDNKPV RSFSSLFLSL RREEKKYSKE RGEKMSRVEV LAKARNERIR EIAIKNREKE
KMKEREKEAK EKEARYTNGH LFNSITVSGL TQCYACNKSI TAKEALICPT CNVTIHNRCK
DTLANCTKVK QKQQKAALVK NSSALQTVAL RNKSTLIKDR PSSAVYLSDS FRQSLLGSRR
GRTTITLSKS VSTTNIAGNW NDDSPLGLRR ILSQSTDSLN IKNRTLSVES LIDEGAEVIY
NQLMGNLETD EKDFEADSWS LAVDTNFLQQ HRKDIIKRQD VIYELIQTEL HHVRTLKIMS
DIFRKGMLED LSMDQTLVHS MFPVLDELSD LHVRFLSQLL ERRKDSLVSN SNKNFVINRL
GDILVTQFSG TNAEQMKKAY KEFCSRHTKA VKLYKELFTR DKRFQQFIRR MTRSTVLRRH
GIQECILLVT QRLTKYPVLI DRILQNTKGN EEDSRDLAQA LSLIKDLIFT VDQEVFECEK
SLRLQEIYNR VDSKAVGVVH GGRLFRKEEF QRRKLIHDGF MLWKNSSGRF KDVQVLLMTD
VLVFLQEKDQ KYTFPSMDKP SVISLQNLIV RDIANQERGI FLISAASPPE MYEILAASKD
ERNTWMKMIK HTVSTCPKRE EFPLIETEDE VLLRNLKDEI QQKDREIQEL LEERVNLFSE
VLQLQASQEV PLNPNSRNLF RSDSANSLKG EKLITEAIKE VEKLKDLLVG GSVELSVSVV
DGDRNECLSS EGTRQHSSDA TNGENGGVNG QPDFRRTSIS VQKDRNGNQL QQRSPQEEVY
QSLVNIYSFL HGLQAVVVQQ DTLLELCIQE VVDKKEKLTR SNSRDGPLGD PGSKTTEKTS
NELNLLQRQH ILLQEELSRC RKACEEKAQE ARELQARLQG SEAAKVALQD SKGQEGGVAH
PEVVMRNKKH SHVRRCSLPS PDLLHLNFTP LQVPQQRRGS DVTVVPLTPT SPLQSNLDCV
PTKEIEDDEV ARLHEQSDLE MNSDTECDGQ RSTPPSPREY QRMQDITEEE EGSQEVREEG
SNPTTDP
//
