ID A0A3B4H2J4_9CICH Unreviewed; 1174 AA.
AC A0A3B4H2J4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=FYVE, RhoGEF and PH domain containing 6 {ECO:0000313|Ensembl:ENSPNYP00000028684.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000028684.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000028684.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR AlphaFoldDB; A0A3B4H2J4; -.
DR STRING; 303518.ENSPNYP00000028684; -.
DR Ensembl; ENSPNYT00000029382.1; ENSPNYP00000028684.1; ENSPNYG00000021583.1.
DR GeneTree; ENSGT00940000156334; -.
DR Proteomes; UP000261460; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15743; FYVE_FGD6; 1.
DR CDD; cd13237; PH2_FGD5_FGD6; 1.
DR CDD; cd00160; RhoGEF; 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); 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF12; FYVE, RHOGEF AND PH DOMAIN-CONTAINING PROTEIN 6; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 627..816
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 845..939
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 975..1034
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1075..1171
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 131808 MW; 2E730E62D0044DDA CRC64;
VTTKPSPPPV APKPGLICQP LAVSQPSPST LKRAKPAVAP KPCIPKYSVQ EAFDDGLNLL
NSKNGILSEA SRRESDYIIP TCSCGLRDCA QCQPLENGST SEAGGHSHKE LLENGVSKEG
FVGSNKEVQR TKEQEVTLKN QESPAAELDV SKVSTEAQNT HLKSACDVIG GIIVFSSISP
LELPTEYSES SNTVSRVSPT QSHPDLQVPA APSKPLPVPQ PRKLKKPALV RQDGLEGGAQ
EQFVEEQKQR TEMKEAEGKL AALSLSTESE ELKPDACDDS SPPKDSGLGD DEADAPVPPP
RQTSLSPHLH RSFRINPNLN KNNSHSLDLL SQPDSVSHSK EGEARRAEED EEDGYGDFER
YPISHSLPKQ IKLSCHPPLA NDRKAFSAEE EQSPRAPPRK PQRHSLPAPP PPSICPPAPP
HANTPMRELP APPQEKTSWR FSRPYVTFFS RQIPTRSSVP PKSRAPVLGC KQRAQSFSAA
DLATRANSPK RSLSFRKLLE LRLSVKMLPK LLAKGGQSLD CTSVESNRGK RSLERPSSCI
GEADICGEGI EGLAEYENVP LYEEIPEYMN LPFHSARLGW PHDPDAADAD IYEVQDPYHR
CQEHEYERYA ALLINFFSQE DEMKRKKVVH IAQEIMSSEK VFVDVLKLLH IDFRDAVAKA
TRQNGKPVVD ERILCQILYY LPQLYQLNKD LLRELEERVA HWSDHQRLSD IFVQKGPYLK
MYSTYIRQFD NNVALLDEQC RKNPAFAAVV REFEMSPRCA SLALKHYLLK PVQRIPQYQL
LLTDYLKNLP EDSEDYKDTQ AALSIVKEVA NHANDIMKQG DNFQKLMQIQ YSLTGHHEIV
QPGRVFLKEG TLMKLSRKVM QPRMFFLFND ALMYTTPVQS AQYKLNSVLS LAGMKVSKPS
QEAYQNELNI ESVERSFILS ASSATERDEW LEAIAKAIDD YTKKKITFIS SRSQEEGVVD
SGAPLGSKAP IWIPDLRATM CMICTCEFTL TWRRHHCRAC GKVVCQACSA NKYYLEYLKN
QPARVCDHCF AKLQENSDRC ASTSISPIKS GAFSFTRKQK KIPAALKEVS ANTENSSMSG
YLNRSKGNKK QWKRLWFVIK NKVLYTYAAS EDVAALESQP LLGFFLREEK NGPAQKLQFK
LYHKNTLFYI FKADDIPTAQ RWIEAFQEAM ILEQ
//