ID A0A1S3LIH3_SALSA Unreviewed; 1170 AA.
AC A0A1S3LIH3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=PH and SEC7 domain-containing protein 4-like isoform X1 {ECO:0000313|RefSeq:XP_013990699.1, ECO:0000313|RefSeq:XP_013990708.1};
GN Name=LOC106566806 {ECO:0000313|RefSeq:XP_013990699.1,
GN ECO:0000313|RefSeq:XP_013990708.1, ECO:0000313|RefSeq:XP_013990716.1,
GN ECO:0000313|RefSeq:XP_013990726.1, ECO:0000313|RefSeq:XP_013990734.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013990726.1};
RN [1] {ECO:0000313|RefSeq:XP_013990699.1, ECO:0000313|RefSeq:XP_013990708.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013990699.1,
RC ECO:0000313|RefSeq:XP_013990708.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane
CC {ECO:0000256|ARBA:ARBA00004632}.
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DR RefSeq; XP_013990699.1; XM_014135224.1.
DR RefSeq; XP_013990708.1; XM_014135233.1.
DR RefSeq; XP_013990716.1; XM_014135241.1.
DR RefSeq; XP_013990726.1; XM_014135251.1.
DR RefSeq; XP_013990734.1; XM_014135259.1.
DR GeneID; 106566806; -.
DR KEGG; sasa:106566806; -.
DR OrthoDB; 204547at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd13295; PH_EFA6; 1.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041681; PH_9.
DR InterPro; IPR001605; PH_dom-spectrin-type.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR10663:SF365; PH AND SEC7 DOMAIN-CONTAINING PROTEIN 1-LIKE ISOFORM X1; 1.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF01369; Sec7; 1.
DR PRINTS; PR00683; SPECTRINPH.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48425; Sec7 domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 660..843
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT DOMAIN 887..996
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..172
FT /note="Basic and acidic 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 235..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1170 AA; 133607 MW; 20CE42B9F63D9AD8 CRC64;
MEEAMVCSPL PDLKEPDSQT WTSMELLPPS RPLEEATRWG EMEKQVNKAD REKEDNSPQT
GRISEEPEEH WDSMTLPVYP MTCPSVLLSF ATVQWDMPDL SPDTPFPMTD NSLADELNSS
GASSLDWTVN PLSLHHHHHQ QQHQSCVTVI NIELSVQEKT EKHNRPEQQL PLDSEESHPP
LLQFQACDTP SPDVEASAQQ LFEEHDSLSE SSPWPETEKG MGQPVTEDTI PPSDRAPSPV
QTGESETGLD SESLDSVLGE EQEQTSKVLT IPINSDQGSS STNYEEKEQA VTNLAYNGDC
DELTEQTEQS EGREQSDSEG ESETIELLEH LFEPAELKEQ SELTEKSEHS GQSEPNHTKQ
SEYKDNTETT EQPEESEQLV ESDQVEHSNQ LGEEEQQTEE THLQHADQSD EIDQSEQSKE
SEQTEQSEQT ECLESKQLQQ TQHSQQTMHS EQTEFSVQTE PQTEPSREME LSEDSEQTKQ
SGETEQTEQS EQTEQSEQTE QSEQTEQSEQ TEQSEQTEQS EQTEQSRDSD QSKQSGETEQ
SEQTEQSEQT EQSEQTEQSE QTEQSEQTEQ SEQTEQSEQT EQSEQTDNKP VHSKQLDLCF
QCTEELEQSD HTEEQKQSEI EQPAQTELTE LTEEDAQTEH FKQVEELEPK EYKEDSCLPP
REGSLEQLES QVQQTEASEP VVVHMNGGDL DREKACRLAE RLYRLDGIHK TDVVKHLDKD
NGFSQAVGQE YLKFFDFTGQ SLDQGLRSFL RVVVLIGETQ ERERVLQHFS CRFQQCNPHT
FSSSGEVLTL TCAVMLLNSD LHGQNVGKAM SVSSFVSNLD GMNEGENFNK ELLKALYNTI
KNEPLEWAVD EKELKSSMLL VEDAKEDAPL RSKSNPFQDV PHDKKATVFK QGFLKRKAHA
DIDGKRTPWG KRSWKTFYGV LKGMVLYLQK DEYRMEWQST EEVVSVHHAL AEQAADYTKR
PHVFRLQTAD WRIFLFQASS TAEMSSWISR INLVSALRSS PPFPAAVGSQ RRFCRPILPA
SQSAQTLERQ LQSHARMLLS FQEDLAYLQQ SLPESRRAKA KELEEHRVRE EYLQHEKCRY
EAYIQMLEAW KGLNQSVDTE VGTSELSLFD RAVCKDPVDE EGKEGTLKKS HSSPSLDLEM
ASPHVVKVKR NISERRTYRK IVIPRRNRDI
//
