SAC2_DANRE
ID SAC2_DANRE Reviewed; 1120 AA.
AC A8E7C5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Phosphatidylinositide phosphatase SAC2 {ECO:0000250|UniProtKB:Q9Y2H2};
DE EC=3.1.3.25 {ECO:0000250|UniProtKB:Q9Y2H2};
DE AltName: Full=Inositol polyphosphate 5-phosphatase F {ECO:0000250|UniProtKB:Q9Y2H2};
DE AltName: Full=Sac domain-containing inositol phosphatase 2;
DE AltName: Full=Sac domain-containing phosphoinositide 4-phosphatase 2 {ECO:0000305};
DE Short=hSAC2;
GN Name=inpp5f {ECO:0000250|UniProtKB:Q9Y2H2};
GN Synonyms=sac2 {ECO:0000250|UniProtKB:Q9Y2H2}; ORFNames=si:dkey-192p21.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Inositol 4-phosphatase which mainly acts on
CC phosphatidylinositol 4-phosphate. May be functionally linked to OCRL,
CC which converts phosphatidylinositol 4,5-bisphosphate to
CC phosphatidylinositol, for a sequential dephosphorylation of
CC phosphatidylinositol 4,5-bisphosphate at the 5 and 4 position of
CC inositol, thus playing an important role in the endocytic recycling.
CC {ECO:0000250|UniProtKB:Q8CDA1, ECO:0000250|UniProtKB:Q9Y2H2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2H2};
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000250|UniProtKB:Q9Y2H2}. Early endosome
CC {ECO:0000250|UniProtKB:Q9Y2H2}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q9Y2H2}. Note=Also found on macropinosomes.
CC {ECO:0000250|UniProtKB:Q8CDA1}.
CC -!- CAUTION: INPP5F has been initially described as an inositol
CC polyphosphate 5-phosphatase. {ECO:0000250|UniProtKB:Q9Y2H2}.
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DR EMBL; BX005252; CAP09243.1; -; Genomic_DNA.
DR EMBL; BX530079; CAP09243.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001119904.1; NM_001126432.1.
DR AlphaFoldDB; A8E7C5; -.
DR SMR; A8E7C5; -.
DR STRING; 7955.ENSDARP00000082038; -.
DR PaxDb; A8E7C5; -.
DR PeptideAtlas; A8E7C5; -.
DR Ensembl; ENSDART00000140634; ENSDARP00000121830; ENSDARG00000061437.
DR GeneID; 570007; -.
DR KEGG; dre:570007; -.
DR CTD; 22876; -.
DR ZFIN; ZDB-GENE-041111-194; inpp5f.
DR eggNOG; KOG1890; Eukaryota.
DR GeneTree; ENSGT00940000155996; -.
DR HOGENOM; CLU_008079_0_0_1; -.
DR InParanoid; A8E7C5; -.
DR OMA; CWRDKQG; -.
DR PhylomeDB; A8E7C5; -.
DR Reactome; R-DRE-1660516; Synthesis of PIPs at the early endosome membrane.
DR PRO; PR:A8E7C5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000061437; Expressed in early embryo and 20 other tissues.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:2001135; P:regulation of endocytic recycling; ISS:UniProtKB.
DR InterPro; IPR034753; hSac2.
DR InterPro; IPR022158; Inositol_phosphatase.
DR InterPro; IPR002013; SAC_dom.
DR Pfam; PF12456; hSac2; 1.
DR Pfam; PF02383; Syja_N; 1.
DR PROSITE; PS51791; HSAC2; 1.
DR PROSITE; PS50275; SAC; 1.
PE 3: Inferred from homology;
KW Coated pit; Endosome; Hydrolase; Membrane; Reference proteome.
FT CHAIN 1..1120
FT /note="Phosphatidylinositide phosphatase SAC2"
FT /id="PRO_0000331623"
FT DOMAIN 167..518
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT DOMAIN 593..760
FT /note="hSac2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01127"
FT REGION 837..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1120 AA; 126054 MW; F034337C693B295C CRC64;
MELFQAKDHY ILQSGDNALW CSRKDGSMAV RPATDLLLAW NPVCLGLVEG IIGKMQLHVD
LPLGLILIRQ KALVGQLPGD HKVYKITKIV VIPLSEDEPQ DLELELCKKH HFGINKPERI
TQSPDETKFL MKTLSQIKSN VGAPIKKKVK ENKEKERLER RLLDELYKIF MDSDSFYYSL
TYDLTNTVQR QGELGKSDQP LWKRVDDRFF WNKHMIKDLV DLQAPQVDFW VIPIIQGFVQ
VEELVVNYNE SSDEERSSPE TPLQEPTCVD DIHPRFTVAL ISRRSRHRAG MRYKRRGVDT
DGHVANYVET EQLIHVHSHT LSFVQTRGSV PVFWSQAGYR YNPRPRIEKG ERETMPYFAS
HFEKEVETYK KLVIINLVDQ NGREKIIGDA YLKQVLLYNN PNLTYVSFDF HEHCRGMKFE
NVQTLTDAIY DIITDMRWAW VDQAGVICQQ EGIFRVNCMD CLDRTNVVQA AIARVIMEQQ
LKKLGVMPPE QPLPLKCYRI YQVMWANNGD TISRQYAGTA ALKGDFTRTG ERKLAGVMKD
GVNSANRYYL NRFRDAYRQA VIDLMMGHPV TEDLYSIFSK EKEHEEKEKE SQRGAQEQVS
LLLQTYMQLL LPDDEKFHGG WALIDCDPSL IDATHKDVDV LLLLSNSAYY VAYYDEEADK
VNQYQRLSLE GLEKIEIGPE PTLFGKPKYC CMRLHYKNGE TSGYFHTLRS VTRNPEDDGK
DTLQCIAEML RITKQAMGLD VQVVEKKLER RHSKPHEDIM GIQGKAVDQV LGSGLAQGKS
FFLNKFSTLN QKVKQTKTNV NIGNFKPLGK LGTFSKPEVK VNFLKPNLHM NLWKSDSSLE
THDSNTGSGA LKDHGPHSEE ISSDSDSYNS DEQPCSGSRE NVDYVLPSCG IVASAPRLGS
RSQSIGSVEI AVPSVIRVTG CDEKTMDSLS VAADQSPGAA SEAEEAILID FGTPIDVYCH
QFVQDAKTKP IEVFEEVAPA PKPQGPQVPL APDAKLGSSH SQNQLPRPSQ LEVESNVHGA
NLLTVQPVGS ATSCGSQKSL EGITGPSSAD SNGSRVVSPF AKIRSSMVQV ASLTQAGLTQ
GINFAVAKVQ KSPEPDAVNE TQENELRAMF TQCQTRIIQI
