ID A0A1S3PN58_SALSA Unreviewed; 2112 AA.
AC A0A1S3PN58;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase {ECO:0000256|ARBA:ARBA00012009};
DE EC=2.7.1.150 {ECO:0000256|ARBA:ARBA00012009};
GN Name=LOC106586374 {ECO:0000313|RefSeq:XP_014029056.1};
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_014029056.1};
RN [1] {ECO:0000313|RefSeq:XP_014029056.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014029056.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014029056.1; XM_014173581.1.
DR STRING; 8030.ENSSSAP00000063983; -.
DR PaxDb; 8030-ENSSSAP00000063983; -.
DR OrthoDB; 5481504at2759; -.
DR Proteomes; UP000087266; Chromosome ssa25.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04448; DEP_PIKfyve; 1.
DR CDD; cd03334; Fab1_TCP; 1.
DR CDD; cd15725; FYVE_PIKfyve_Fab1; 1.
DR CDD; cd17300; PIPKc_PIKfyve; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR043548; PIKfyve.
DR InterPro; IPR037378; PIKfyve_DEP.
DR InterPro; IPR044769; PIKfyve_PIPKc.
DR InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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; PTHR46715; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE; 1.
DR PANTHER; PTHR46715:SF1; 1-PHOSPHATIDYLINOSITOL 3-PHOSPHATE 5-KINASE; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01504; PIP5K; 2.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 171..231
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 393..468
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 1763..2098
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1762..1820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1762..1797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1802..1820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2112 AA; 237414 MW; 0E56096F75C0DDD8 CRC64;
MAADDKSSSS SSTLDWSVAP PISPGSPSHL THFKPLTPEQ DEPPLRSAYS SFVNLFRFNK
EEGRPPSVTE KPDVVVASPT GERRNWTIPA HSIHGPGAHR KQHHDLLRRT STASVDWPLW
PGEEGRRKSE TPLGTHDPRT AVQLRTALKR LKEIMEGKSQ DSDLKQYWMP DSQCKECYDC
NEKFTTFRRR HHCRLCGQIF CSRCCNQEIP GKFMGYTGDL RACTYCRKIA LSYSHSADSG
SIGEDLSALS DSSPCSTCVL EPSEPRTPVG GRKASRNIFL EEDLAWQRKT PIGMRKNLIH
QESQNSGMNS RRSTLQEDGG KSPIRKRPVL SRSASVTNLS LDRSGSSMVP SYDSSVSPQT
SRAMPKPDHS EEERKILLDS SQLKDLWKKI CHNTTGMEFQ DHRYWLRTYP NCIVGKELVN
WLLRNGTIST RAQAIAIGQA LVDGRWLDCV THHDQLFRDE YALYRPLQST DFSETPSPDS
DSVNSLEGHS EPSWFKDIKF DDSDTDQVAD ENDYVMPNSS SPSKRTSVSS FQSAVDSDSA
ASINLNMEQD NVNFHIKKQS KYPHVPPHPT EQKEYLVSED GGQNISISDA FIKESLFNRR
VEEKAKEMLF TPLGWHHSSL DQLREENGEK KAMERLLSAN HSHMMALLQQ LLYSESLSLS
WRDIIVPVVR QVVQTVRPDV RSCDDDMDIR QLVHIKKIPG GKKFDSAVVN GFVCTKNIAH
KKMNSYIKNP KILLLKCSIE YLYREETKFT CIDPIVLQER EFLKNYVQRI ADVRPNLVLV
EKTVSRIAQD MLLEHGITLV INVKPQVLDR VSRMTQGDLV MSMDQLLTKP RLGTCQKFYL
HSFQLANNEL KTLMFFEGCS PQLGCTIKLR GASEYELARV KEIIVLMVCV AYHSQLEISF
LMDEFAMPPS LAKTNSFPCL LERTTVEEEE SQENGTDQST LSQGGETVLG EEEEKPSLGK
SVSESSSPKD VHGVKVNKKH FLSSSSSLGA EGVESSEVMT STPLSNRQVL PPPVSPPYLI
DDLEELADEI GSGKGETEGG SGSGVLGRGE SREESSGSET PPRLFRDPLQ DDTGLFVTEQ
VASTDDRLKT LTAGFKQELK DIILCISPFI TFREPFLLTP AGLRCPSRDY FPEKVYLSPL
LNKDFKELDC RRKRQLLKDS APSGGGIANG VPPPRPIQVL PSHHLTSARI AEQLGSSQDL
AKMLADYRAQ GGRLRQEADP FTQPLPQPPV REAPPPKHPI KADSEEEKPA GQNDMTWASK
LDCLNPVNHQ RLCVLFSSSS AQSNNSPNPC VSPWIVTMEF YGKNDLTLGI FLERYCFRPS
YQCPSMFCET PMVHHVRRFV HGSGCVQIVL KELDSPVPGY QHTILNYSWC RICKQVTPVV
PLSNDSWSMS FAKYLELRFY GHQYTRRANA EPCGHSIHKD YHQYFSYNQM VASFSYISVR
LLEICLPPPK IFIRNQGPSK GSMQQDLKDF SQNVNQVYLA IEDRLTSLKT DTFSKTREEK
MEDLFAQKDM EEAELRSWIE KLQARLQACG SDSPQQLQTV LESVVVKKQS LCETLQSWNS
RLQDLFQQEK GRKRLSVPAS PGRHRQTDDS KTSVLESSPR NPSPVVQNGD KEDRHLTTLP
SSSGSSLLTL PSPGEPGSEP LSSGPSFPDQ DSVSIPEDVF DGHLLGSNDS QVKEKSTMKA
ILANLLPGNS YNPIPFPFLN PSVDGKNHRY ISDPDKHYLM YEHERVPIAV CEREPSSIIA
FALSCKEYKT ALDELSKTTV KAGGEDTTQT ISSGESRAKN SPAKPNETAS SQMGAGRSSM
DADPLKDADI GDKHKKSAGN PHIELQFSDA NAKFYCRIYY AEEFHKMREE IMDSTEDDFV
RSLSHCVNWQ ARGGKSGAVF YATEDDRFIL KQMPRLEVQS FLDFAPHYFT YITGAVQQKR
PTALAKILGV YRIGYKNSQN NSEKKLDLLV MENLFYGRKM AQVFDLKGSL RNRNVKTDSG
KESCEVVLLD ENLLKLVHDN PLYIRAHCKA ILRAAIHSDA YFLSSHLIID YSLLVGRDDT
TDQLVVGIID YIRTFTWDKK LEMVVKSTGI LGGQGKMPTV VSPELYRSRF CEAMDKYFLM
VPDHWTGLGV NC
//