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Database: UniProt
Entry: A0A1S3N0A7_SALSA
LinkDB: A0A1S3N0A7_SALSA
Original site: A0A1S3N0A7_SALSA 
ID   A0A1S3N0A7_SALSA        Unreviewed;      1366 AA.
AC   A0A1S3N0A7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=FYVE, RhoGEF and PH domain-containing protein 6-like {ECO:0000313|RefSeq:XP_014008862.1};
GN   Name=LOC106576296 {ECO:0000313|RefSeq:XP_014008862.1};
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_014008862.1};
RN   [1] {ECO:0000313|RefSeq:XP_014008862.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014008862.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
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DR   RefSeq; XP_014008862.1; XM_014153387.1.
DR   STRING; 8030.ENSSSAP00000065073; -.
DR   PaxDb; 8030-ENSSSAP00000065073; -.
DR   Ensembl; ENSSSAT00000237717; ENSSSAP00000170433; ENSSSAG00000058619.
DR   GeneID; 106576296; -.
DR   KEGG; sasa:106576296; -.
DR   OMA; EDRVAHW; -.
DR   OrthoDB; 5385125at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa17.
DR   Bgee; ENSSSAG00000058619; Expressed in camera-type eye and 14 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   PRINTS; PR01217; PRICHEXTENSN.
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:UP000087266};
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          818..1007
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1036..1130
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1168..1227
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          1269..1365
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          671..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          778..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..32
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..87
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..324
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..375
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..404
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..575
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1366 AA;  151558 MW;  C333E1BDE3E9F00B CRC64;
     MSTGVKKPPV APKPKLAPLV KLSPPPIAPK PDLLLSQPSQ PSPLLTQPSP AVLKRAKPAV
     APKPCLSKPS APAAPASPPP PRPRVPQTPS QECSGAGDDS LSFLNSRNGI LSQPILHDSD
     YIIPTCSCGL QDCSQCKRLG NGNVTEVGSD TLGSWPNRNA TESTGTLVAN RPGKTENGDS
     EKSGGVTNTL RLRLKDKPQR QEGQRDGEGS RDEEKLQGNK EERPRNQKGQ EGQQYQTGSG
     DQSCNVPEVA ETLTQTETKA SNAERTYTDS CNIDSNESDT IPTPLILPLD VSPIHTPPQT
     VPPTRTPSQT VPPTRSPPQI LPPSLTPTQM DSEPDSTPSH ADSSTQCSRI PRLPTDLSVP
     AAPSKPLPVP LPRKPRKPAL VRQDGLEAST QEGETKNRTQ GGEVGETEGS GGRCLTSDKE
     EHTQGVYDSP SPSQDPEVEE EPHPVPPPRQ KSLSPRLHRA SLNRNTSHSL DLLSQPELNA
     LTSERRGGGD EEEEKEEEVE DGYGDFERYP ITRSLPKQIK LSCRPPPVGM TMKASSAEEG
     GSPRAPPRKP QRHSLPAGAP PSITPPPPPP HHANTPMREL PATPQEKPAW RFPRPFFSRQ
     SSSRHSSGGR GAPQGKAALL GGKQRAQSFS SADLLARADG TKRSLSFRKL LELRLSVRML
     PRLLARSGQS LDCTSVEPGG GGRTVDQSDG SAGVSGRDGE GSVEYENVPL YEEIPEYMNL
     PFLSARLGWP LTHSLDPSTH RHSDSDVYEV QDPYESHCDY KRPHSIDYER GWHGLDDAHS
     EEEVHSSDED DNSSTSSKEH LELSEEDRQQ EDEVKRKKMV HIAQEIMSSE KVFVDVLKLL
     HIDFRDAVAK ATRQNGKPVV EERILTQILY YLPQLYQLNR DLLRELEERV ARWGDHQRLA
     DIFVQKGPYL KMYSTYIRQF DNNVAMLDEQ CRKNPGFAAV VREFEMSPRC ASLALKHYLL
     KPVQRIPQYQ LLLTDYLKNL PEDSSDYKDT QAALGIVKEV ANHANDIMKQ GDNFQKLMHI
     QYSLNGQHEI VQPGRVFLKE GTLMKLSRKV MQPRMFFLFN DTLLYTTPVQ SGQYKLNSML
     SLAGMKVSKP SQEAYQNELN IESVERSFIL SASSATERDE WLAAIATAID DHTRKKITFI
     SSRSQEEADG VCDSGAPLGS KAPIWIPDLR ATMCMVCTCE FTLTWRRHHC RACGKVVCQT
     CSSSKFYLEY LKNQPARVCD HCFVKLQENS DRVASGALSP TGRSGGFSFS RKQKKIPAAL
     KEVSANTENS SMSGYLQRSK GNKKQWKRLW FVIKNKVLYT YAASEDVAAL ESQPLLGFFL
     REEKCGPFQK LQFKLYHKNT LFYIFKADDI PTAQRWIEAF QEAMIL
//
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