ID A0A2U9B302_SCOMX Unreviewed; 1276 AA.
AC A0A2U9B302;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 03-MAY-2023, entry version 18.
DE SubName: Full=Putative FYVE RhoGEF and PH domain-containing protein 6-like {ECO:0000313|EMBL:AWO98247.1};
GN ORFNames=SMAX5B_010634 {ECO:0000313|EMBL:AWO98247.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWO98247.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWO98247.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; CP026244; AWO98247.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9B302; -.
DR STRING; 52904.ENSSMAP00000009289; -.
DR Proteomes; UP000246464; Chromosome 2.
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:UP000246464};
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 727..916
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 945..1039
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1077..1136
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1177..1273
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..32
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..493
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..699
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 142280 MW; 104E9DE8840E96EC CRC64;
MSTGVKKPPL APKPKLPATA KPSPPPIAPK PGIVLTQSPA VSQPSPATLK RAKPALAPKP
CIPKSLASSP PPPPKPAGAL IISQEQQEAL DNSLSLLNSR NGILSESHKR ESDYIIPTCS
CGLRDCSQCR RLENGSVTEI GGGDLHREPQ RNGVSTEGLA GTGMGPQEKA ETRGEGVAAQ
KGEAGGISKK PRDKPQRHRH LDREAQREKV SEAVKHQESA EPEQTEDQNT DLTDSPPACD
VAGSIIVFSS ITLSAESFQV EYDEPFRDAC PARLPPELQV PAAPSKPLPV PHPRKHKKPA
LVRQDGVEGS GAQDPSAEER AQGTEVREAE GRLSLAGLSE GGELTQDTSD DSLPQKDSGM
EDSESDAPVP PPRQTSLSPR LHRTVHAPHC LNKNTSHSLD LLSQPDSASH KTEGEDRRAE
DDEEDGYGDF ARYPITHSLP KQIKLGCHPK ALSAEDQPFP RAPPRKPQRH SMPAAPPPSI
CPPAPPHANT PMRELPAPPQ EKTAWRFTRP CVTFFSRQMP TRSSVPPKGR APALGGKQRA
QSFSAADLAT RANSQKRGLS FRKLLELRLS VKMLPKLLAK GGQSLDCTSV ESTRGERSQE
RPNSCIGGAA DICGEGVDES VEYENVPLYE EIPEYMNLPF HGARLGWPGD LEAADSDIYE
VQDPYHRCRD HEYESDWLGQ DVHSEEDEEE EEEEIHSSDE EDSSSTSSKE HLDEADRQQE
DEMKRKKVVH IAQEIMSSEK VFVDVLKLLH IDFRDAVAKA TRQNGKPVVD ERILNQILYY
LPQLYQLNRD LQRELEERVA HWSDHQRLSD IFVQKGPYLK MYSTYIRQFD NNVALLDEQC
RKNPAFAAVV REFETSPRCA SLALKHYLLK PVQRIPQYQL LLTDYLKNLP EDSEDYKDTQ
AALSIVKEVA NHANDIMKQG DNFQKLMQIQ YSLNGHHEIV QPGRVFLKEG TLMKLSRKVM
QPRVFFLFND ALMYTTPVQS GQYKLNSVLS LAGMKVSKPS QEAYQNELNI ESVERSFILS
AGSATERDEW LEAIAKAIDD YTKKKITFIS SRSQEEAECV VDSGAPLGSK APIWIPDLRA
TMCMMCTCEF TLTWRRHHCR ACGKVVCQAC SANKYYLEYL KNQPARVCDH CFAKLQENSD
RCASTSVSPI KSGAFSFTRK QKKIPAALKE VSANTENSSM SGYLNRSKGN KKQWKRLWFV
IKNKVLYTYA ASEDVAALES QPLLGFFLRE EKNGPAQKLQ FKLYHKNTLF YIFKADDIPT
AQRWIEAFQE AMILEQ
//