ID A0A3P8TL27_AMPPE Unreviewed; 1237 AA.
AC A0A3P8TL27;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=FYVE, RhoGEF and PH domain containing 5a {ECO:0008006|Google:ProtNLM};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000023762.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000023762.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000023762.1}
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; A0A3P8TL27; -.
DR Ensembl; ENSAPET00000024391.1; ENSAPEP00000023762.1; ENSAPEG00000016777.1.
DR GeneTree; ENSGT00940000157922; -.
DR Proteomes; UP000265080; Chromosome 6.
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 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; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF13; FYVE, RHOGEF AND PH DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF01363; FYVE; 1.
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; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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:UP000265080};
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 745..916
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 939..1236
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1058..1117
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1237 AA; 138925 MW; 725B17BA8DC21CCD CRC64;
MDAEGCDAGE ALADTDGLSV GDFSVNSIDE KAGCCSPEKQ DTEEKQENNP TSEDGSTADD
LTESLTDESG LLVKENTDTQ HVFLTEEEEK ETASDCGFTC NILKLRCGHK TKERDENLQN
ICFNDVVPED QKKVCDAIKK HADLVRDPAH EPFYISSEDI INRELMPRSD KAYGLLESGL
KQTSSINCSG GSSWNYKETA ENAQCVASVD FEGTGDGDEN KVRTCQKRMS VKTEELNSHA
VEDVLDHLDC QPRFRLVSIS VPTDTDTPLS SSVSESQLLS PNDSDVFRDE DDLEGHIVPF
LDDTTDTEQD ISDEHVYEEP GHSLEADGVF PFDRRATGIR SGSVSQRNTN HVEDLGVQFF
QKPYMSGFGQ SALCSSPMLN SARHKSYSKP HYLSLYPRSL SMEGHDMPLG VYREGSPRQR
GAFCSSESFS RCSPLSSSAV STPTSVVDIP PPFELAYITQ RPITKSSPSL LIEGDLSEKN
RKKKSSIKRF LMLKFKWKTE NKQVVDVNPS SSKSPEESSH HTPSRLLDLD RHSISSSPQL
SSLSASKPQG SPDPASPFLL YKESKRKGNA VAFLNRSVVR VESFEDRSRV PFTPLPLTKP
RSISFPNTDT SDYENVPPIS SDYENLQVPQ RRPVRQAPFT GFFDRPSRVL SSANETDGYV
DMSSLPGFEK KTQSPEQETE SAYTEAYNVC LMAVGPRTGS VGDGGREMVG EEDLGRTSEE
EDGGTDNSYD RQHCDLNYKI TSIPLHSAVC QDFREAVGST VGDEGEPVLD DERLREILNE
LPDVYSLHRT ILAELENRIR YWGERQRIAD IFLSRKAEFL VFTTYIGHYD RSMSLLEDSC
RTSSAFAAIV QQFEQSLAGE KVSVKHQLLQ VIVRVAQYRM LLTDYLNNLS PDSQEYEDTQ
GTVNMLQEQT SVQTENLLRL VNIEYSVRGQ RDLLQPGRVF VKEGTLMKVS RKSRQPRHLF
LMNDVLLYTY PQQDGKYRLK NTLPLTGMKV SLSSSHIICS EFVCFFCSSF LEREDWFYTL
NRAVTEHTRG SSAFSCSGEA RDGLRLSLGE KAPTLVPVSQ VMMCMNCTSD FSLTLRRHHC
HGCGRIVCRS CSRNRYPLKY MKDRMAKVCD HCYSELKKRG ERKLFVFAGG DVSALSAKGS
PRVSRSSRPL STVFQNIHPP NIWRHRKGAL SFNQEKVASE SLPLLGFTVK LPDRPERDEE
ASVFQLYHKN TLYYTFKAED NYTAQRWVDA MEEATVL
//
