ID A0A2K6FJC9_PROCO Unreviewed; 752 AA.
AC A0A2K6FJC9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Rho guanine nucleotide exchange factor 4 {ECO:0008006|Google:ProtNLM};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000014084.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000014084.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K6FJC9; -.
DR STRING; 379532.ENSPCOP00000014084; -.
DR Ensembl; ENSPCOT00000024691.1; ENSPCOP00000014084.1; ENSPCOG00000018711.1.
DR GeneTree; ENSGT00940000160622; -.
DR OMA; ACMRTQQ; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd01224; PH_Collybistin_ASEF; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11973; SH3_ASEF; 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; IPR035899; DBL_dom_sf.
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; PTHR47544; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 4; 1.
DR PANTHER; PTHR47544:SF1; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 4; 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; SM00326; SH3; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 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 Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 256..315
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 346..530
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 561..668
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 85358 MW; EA0ADA9884EEE4F0 CRC64;
MVSLGSYSDV DSSSGAPESP KIPKTRTSLL LSLQTINQAG QKEERGKRGQ RPRGLSTAPS
LRDLPGSENH KPWEELLGEK PSCSCGQKAV HAEPAQGPGP TTERITWILP REAPVPPRSI
AHCPPISLDD LWLEKMQRKK LEKQAQAEPR MQAGAAHRDG VQCWRKTIIT SAESLDLSRS
SCPLSQSAPT GLNHVGWPEH IPDTAMPDGA LDAAMRADEA GSEEDLYEDL HGSGHHYSHP
GGGGEQLAIN ELISDGSAVC AEALWDHVTM DDQELGFKAG DVIEVMDATN REWWWGRVAD
GEGWFPASFV RLRVNQDEPG DDEAPRPGDG EARDSGTEAQ SSKDQMRTNV INEILSTERD
YIKHLRDICE GYLRQCRKRA DMFSEEQLRT IFGNIEDIYR CQKAFVKALE QKFNRERPHL
SELGACFLEH QADFQIYSEY CNNHPNACVE LSRLAKLSKY VYFFEACRLL QKMIDISLDG
FLLTPVQKIC KYPLQLAELL KYTHPQHRDF KDVEAALHAM KNVAQLINER KRRLENIDKI
AQWQSSIEDW EGEDLLVRSS ELIYSGELTR VTQPQAKSQQ RMFFLFDHQL IYCKKDLLRR
DVLYYKGRLD MDGLEVVDLE DGKDRDLHVT VKNAFRLHCG TTGDSHLLCT RKPEQKQRWL
KAFAREREQV RLDQETGFSI TELQRKQAML NASKQQATGK PKAVGRPCYL TRQKHPALPS
SRPQPQVLVL AEPRRKPSTF WHSISRLAPF RK
//