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Protein

Phosphatidylinositide phosphatase SAC1-B

Gene

sacm1lb

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Phosphoinositide phosphatase that hydrolyzes phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 4-phosphate (PtdIns4P) (By similarity). Has low activity towards PtdIns(3,5)P2 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

ReactomeiR-DRE-1483248. Synthesis of PIPs at the ER membrane.
R-DRE-1660514. Synthesis of PIPs at the Golgi membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositide phosphatase SAC1-B (EC:3.1.3.-)
Alternative name(s):
Suppressor of actin mutations 1-like protein B
Gene namesi
Name:sacm1lb
ORF Names:si:ch211-222e23.8
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 19

Organism-specific databases

ZFINiZDB-GENE-060503-122. sacm1la.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei55 – 7521HelicalSequence analysisAdd
BLAST
Transmembranei520 – 54021HelicalSequence analysisAdd
BLAST
Transmembranei548 – 56821HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 586586Phosphatidylinositide phosphatase SAC1-BPRO_0000317176Add
BLAST

Proteomic databases

PaxDbiA4VCH0.

Expressioni

Gene expression databases

BgeeiA4VCH0.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000083973.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini121 – 450330SACPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 SAC domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1889. Eukaryota.
COG5329. LUCA.
GeneTreeiENSGT00530000063393.
HOGENOMiHOG000189112.
HOVERGENiHBG108454.
InParanoidiA4VCH0.
OMAiANAYERF.
OrthoDBiEOG73803W.
PhylomeDBiA4VCH0.
TreeFamiTF313543.

Family and domain databases

InterProiIPR002013. SAC_dom.
[Graphical view]
PfamiPF02383. Syja_N. 1 hit.
[Graphical view]
PROSITEiPS50275. SAC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A4VCH0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANAYERFNL HSTPEKFYIE ACDDGADDVL VIDRVSTEMT LAGIKDIPPS
60 70 80 90 100
GITRPICGVM GTVRLVAGMY LIVITRKRKV GDLFGHTVWK AVEFDVISYK
110 120 130 140 150
KTILHLTDIQ MQDNKTFLTM INNVLNTDGF YFCTDYDLTH TQQRLSNTSP
160 170 180 190 200
DFQEMSLLER ADQRFMWNGN LLREIIAQPE LHKFAFPVIH GFIVMKPCCI
210 220 230 240 250
NGKVFEWIII SRRSCFRAGV RYYVRGIDSE GHAANFVETE QIVQFNNARA
260 270 280 290 300
SFVQTRGSIP FFWSQRPNLK YKPKPLISKD TNHMDGLRRH FESQVLIYGK
310 320 330 340 350
QVILNLVNQK GSELPLEQAF AKMVSSMENG FIKYIAFDFH KECSKMRWHR
360 370 380 390 400
LQILVDAVSD MQEEFGYFMV SSDGKVLSEQ SGTFRSNCMD CLDRTNVIQS
410 420 430 440 450
LLARRSLQSQ LQRMGVLHVG QKIEEQADFE KIYKNAWADN ANACAKQYAG
460 470 480 490 500
TGALKTDFTR TGKRTHWGLV MDGWNSMIRY YKNNFSDGFR QDSIDLFLGN
510 520 530 540 550
YSVDETDSLT PLHVKKDWKF LLLPVIMVVA FSMCIICLLM AGDTWTETLA
560 570 580
YVLFWGMASA LTAAVIVVNG REFVDAPKLV QKEKMD
Length:586
Mass (Da):67,120
Last modified:February 5, 2008 - v2
Checksum:i40BEC53DFAE17188
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti360 – 3601D → E in AAI39690 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR933768, BX537337 Genomic DNA. Translation: CAK04253.1.
BX537337, CR933768 Genomic DNA. Translation: CAK04562.1.
BC139689 mRNA. Translation: AAI39690.1.
RefSeqiNP_001038343.1. NM_001044878.1.
UniGeneiDr.72423.

Genome annotation databases

EnsembliENSDART00000089540; ENSDARP00000083973; ENSDARG00000015290.
GeneIDi558940.
KEGGidre:558940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR933768, BX537337 Genomic DNA. Translation: CAK04253.1.
BX537337, CR933768 Genomic DNA. Translation: CAK04562.1.
BC139689 mRNA. Translation: AAI39690.1.
RefSeqiNP_001038343.1. NM_001044878.1.
UniGeneiDr.72423.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000083973.

Proteomic databases

PaxDbiA4VCH0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000089540; ENSDARP00000083973; ENSDARG00000015290.
GeneIDi558940.
KEGGidre:558940.

Organism-specific databases

CTDi558940.
ZFINiZDB-GENE-060503-122. sacm1la.

Phylogenomic databases

eggNOGiKOG1889. Eukaryota.
COG5329. LUCA.
GeneTreeiENSGT00530000063393.
HOGENOMiHOG000189112.
HOVERGENiHBG108454.
InParanoidiA4VCH0.
OMAiANAYERF.
OrthoDBiEOG73803W.
PhylomeDBiA4VCH0.
TreeFamiTF313543.

Enzyme and pathway databases

ReactomeiR-DRE-1483248. Synthesis of PIPs at the ER membrane.
R-DRE-1660514. Synthesis of PIPs at the Golgi membrane.

Miscellaneous databases

NextBioi20882706.
PROiA4VCH0.

Gene expression databases

BgeeiA4VCH0.

Family and domain databases

InterProiIPR002013. SAC_dom.
[Graphical view]
PfamiPF02383. Syja_N. 1 hit.
[Graphical view]
PROSITEiPS50275. SAC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tuebingen.
  2. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiSAC1B_DANRE
AccessioniPrimary (citable) accession number: A4VCH0
Secondary accession number(s): Q1L8A6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: November 11, 2015
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.