ID A0A498MZ01_LABRO Unreviewed; 1051 AA.
AC A0A498MZ01;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 03-MAY-2023, entry version 14.
DE SubName: Full=PH domain-containing 4-like protein {ECO:0000313|EMBL:RXN24722.1};
GN ORFNames=ROHU_022027 {ECO:0000313|EMBL:RXN24722.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN24722.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN24722.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN24722.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN24722.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN24722.1}.
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DR EMBL; QBIY01012520; RXN24722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498MZ01; -.
DR STRING; 84645.A0A498MZ01; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
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; cd15741; FYVE_FGD1_2_4; 1.
DR CDD; cd15791; PH1_FDG4; 2.
DR CDD; cd13236; PH2_FGD1-4; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 3.
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; IPR037742; FDG4_N_PH.
DR InterPro; IPR035941; FGD1-4_PH2.
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:SF98; FYVE, RHOGEF AND PH DOMAIN-CONTAINING PROTEIN 4; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00169; PH; 3.
DR Pfam; PF00621; RhoGEF; 2.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 3.
DR SMART; SM00325; RhoGEF; 2.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF50729; PH domain-like; 3.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 3.
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 Reference proteome {ECO:0000313|Proteomes:UP000290572};
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 278..465
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 471..677
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 494..593
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 706..805
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 844..904
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 930..1027
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 32..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1051 AA; 119371 MW; 3486481E1AA5FCF9 CRC64;
MDVETDKSGN PSCFPSKQSD EEELCVGVKI AQNKAVGSSS PDEQGHRSEK LSRGCRFSNK
SLTGVNGRVS GRRPPVHPKP QVPPKPAHLQ SPVTEVSFPL AAGTSPINPN MEGGVGGGAI
GKGLVSNLIS RFEENSHTDS RREGAPLKQV SRSPNCSPAH KNCQRQTEQP TDSGSAANTP
RHALKPPNGV LAQKNRERDK NQDMDGVTHD TVPDVRIDRQ ELVNGDAGDV AKREIMDEDC
VDPPHAHIQA EEEERKAPEQ GDVVMNSVPE QKETNEQKLY KIANELLQTE KAYVARLNLL
DKVFYTKLLE EAKKDTFPMD VVKNIFSNIT SINTFHSQFL LPDLEKRMGE WTTTPRIGDI
LQKLTPFLKM YAEYVRNFDH AMELLKLWTD RSPPFKAIIL EIQGQEVCGC LTLQHHMLEP
VQRVPRYEML LKDYLKKLPQ DHIDRRDAEK SLEIIAMAAT HSNTAIRKTE NLKKLLEIYE
MLGEEEDVVN PSNELIKEGH ILKLAARNTS AMDRYLFLFN NMLLYCVPKF SLVGQKFTVR
TRIGIDGMKV TETYNDDYPH TFQVSGKERT LELQASSEQD KESWIKAFDE TIHIYLQKNE
TFKSAFKDVE EVPVSGQEVC GCLTLQHHML EPVQRVPRYE MLLKDYLKKL PQDHIDRRDA
EKSLEIIAMA ATHSNTAIRK TENLKKLLEI YEMLGEEEDV VNPSNELIKE GHILKLAARN
TSAMDRYLFL FNNMLLYCVP KFSLVGQKFT VRTRIGIDGM KVTETYNDDY PHTFQVSGKE
RTLELQASSE QDKESWIKAF DETIHIYLQK NETFKSAFKD VEEVPVSDLK ISELGKRAPR
WIRDNEVTMC MRCKEAFNAL TRRRHHCRAC GYVVCAKCSD YKASLEYDGN RMNKVCKDCY
SIMRGHIDGE EREGKKKGIL EIEAAQFSGN SIMCGFLQYC EKNKPWQKVW CVIPQKEALV
LYLYGAPQDV KAQSTIPLLG YQVDDSPRPT DPPASFRLSQ SKSVHSFAAE SEELKKRWLK
VIRMAVTGEV PESPEENHST EITEEPSSNG V
//
