ID A0A3P8XA95_ESOLU Unreviewed; 1333 AA.
AC A0A3P8XA95;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=FYVE, RhoGEF and PH domain containing 6 {ECO:0000313|Ensembl:ENSELUP00000001539.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000001539.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000001539.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000001539.2}
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 STRING; 8010.ENSELUP00000001539; -.
DR Ensembl; ENSELUT00000017218.2; ENSELUP00000001539.2; ENSELUG00000003018.2.
DR GeneTree; ENSGT00940000156334; -.
DR Proteomes; UP000265140; LG23.
DR Bgee; ENSELUG00000003018; Expressed in heart and 13 other cell types or tissues.
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 Reference proteome {ECO:0000313|Proteomes:UP000265140};
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 785..974
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1003..1097
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1135..1194
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1236..1332
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..75
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..353
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..548
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1333 AA; 148478 MW; C911D4BB0987A412 CRC64;
MSTGVKKPPV APKPKLAPST KPSPPPIAPK PDLLSQPSQP SPATLKRAKP AVAPKPRIPK
PSGLSTPPAS KPLPPQTPTQ AGDINLTLLN SRNGILTESR HLDYVIPICS CGLRDCSQCR
RLGNGNATEV GSVTPDSPKR KATESPETQE EGEKRGVTTK LTSKDKEQRH EGQRNGDGNG
GDGDGNAAQR SLKGQQGHAR SGDQWCNARE VAETWTLSQA DTDTEAVNAP ETLTETDTPN
EQLTHAESQN MDINDSNAVP PSLTPLLVDP PSLTPLQTLP LSLTPPQTVP PTRTPPQITP
PTLAFSQANG ESDGSPSPAE STAHSSRTPR LPLDLSVPAA PSKPLPVPLP RKPRKPVLVR
QNGLEAETHS RTQEEDVGRS EWSGGRGLTS EQEEQEHTEV MYCTPPTQDP QIEEEHHPVP
PPRQKSLSPR LHRGAHCSPL LHRNASHSLD LLSEPDALTS DRRGEEEEKE EEGGYGDFER
YPVSRSLPKQ IKLSCRLPPV GTTPQAQSAE EAGSPRAPPR KPQRHSLPAG APPPVTPPPP
PHHANTPMRE LPAPPQEKAA WRFPRPFFSR QSSSRHSSGG GHTGAPRGRA ALLGGKQRAQ
SFSSADLLAR GDNTKRSLSF RKLLELRLSV KMLPRFLARS GQSLDCTGGE RTADRSNSST
ALSDGIGEGE ELVEYENVPL YEEIPEYMNL PFLSARLDWP HTHRRDPSTH RHSDSDVYEV
QDPYGHYERP HSVDYERGWH GLDDAHSEEE VHSSDEDDNS STSSKEHLEL SEEDRQQEDE
VKRKKVVHIA QEIMSSEKVF VDVLKLLHID FRDAVAKATR QNGKAVVEER VLTQILYYLP
QLYQLNKDLL RELEERVAHW GDHQRLADIF VQKGPYLKMY STYIRQFDNN VALLDEQCRK
NPGFSAVVRE FEMSPRCASL ALKHYLLKPV QRIPQYQLLL TDYLKNLPMD SSDYKDTQAA
LGIVKEVANH ANDIMKQGDN FQKLMQIQYS LNGQHEIVQP GRVFLKEGTL MKLSRKVMQP
RMFFLFNDTL LYTTPVQSGQ YKLNSMLSLA GMKVSKPSQE AYQNELNIES VERSFILSAS
SATERDEWLA AIATAIDDHT RKKITFISSR SQEESDGVCD SGAPLGSKAP IWIPDLRATM
CMICTCEFTL TWRRHHCRAC GKVVCQTCSS NKYYLEYLKN QPARVCDHCF AKLQENSDRV
ASAALSPGGR SGAFSFSRKH KKIPAALKEV SANTENSSMS GYLQRSKGNK KQWKRLWFVI
KNKVLYTYAA SEDVAALESQ PLLGFFLREE KCGPFQKLQF KLYHKNTLFY IFKADDIPTA
QRWIEAFQEA MIL
//
