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PIGW_MOUSE
ID   PIGW_MOUSE              Reviewed;         503 AA.
AC   Q8C398; Q8C4S0; Q9CSX1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Phosphatidylinositol-glycan biosynthesis class W protein {ECO:0000305};
DE            Short=PIG-W {ECO:0000305};
DE            EC=2.3.-.- {ECO:0000250|UniProtKB:Q7TSN4};
GN   Name=Pigw {ECO:0000312|MGI:MGI:1917575};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: Required for the transport of GPI-anchored proteins to the
CC       plasma membrane. Probable acetyltransferase, which acetylates the
CC       inositol ring of phosphatidylinositol during biosynthesis of GPI-
CC       anchor. Acetylation during GPI-anchor biosynthesis is not essential for
CC       the subsequent mannosylation and is usually removed soon after the
CC       attachment of GPIs to proteins. {ECO:0000250|UniProtKB:Q7TSN4}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000250|UniProtKB:Q7TSN4}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q7TSN4}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q7TSN4}.
CC   -!- SIMILARITY: Belongs to the PIGW family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC38199.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK011762; BAB27826.3; -; mRNA.
DR   EMBL; AK081337; BAC38199.1; ALT_FRAME; mRNA.
DR   EMBL; AK086537; BAC39687.1; -; mRNA.
DR   EMBL; AL645623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS36263.1; -.
DR   RefSeq; NP_001071104.1; NM_001077636.1.
DR   RefSeq; NP_081664.2; NM_027388.2.
DR   RefSeq; XP_006534222.1; XM_006534159.2.
DR   AlphaFoldDB; Q8C398; -.
DR   STRING; 10090.ENSMUSP00000064547; -.
DR   GlyGen; Q8C398; 1 site.
DR   PhosphoSitePlus; Q8C398; -.
DR   PaxDb; Q8C398; -.
DR   PRIDE; Q8C398; -.
DR   ProteomicsDB; 288162; -.
DR   Antibodypedia; 74148; 100 antibodies from 23 providers.
DR   DNASU; 70325; -.
DR   Ensembl; ENSMUST00000067058; ENSMUSP00000064547; ENSMUSG00000045140.
DR   Ensembl; ENSMUST00000108080; ENSMUSP00000103715; ENSMUSG00000045140.
DR   GeneID; 70325; -.
DR   KEGG; mmu:70325; -.
DR   UCSC; uc007kqy.1; mouse.
DR   CTD; 284098; -.
DR   MGI; MGI:1917575; Pigw.
DR   VEuPathDB; HostDB:ENSMUSG00000045140; -.
DR   eggNOG; KOG0411; Eukaryota.
DR   GeneTree; ENSGT00390000013520; -.
DR   HOGENOM; CLU_020802_2_2_1; -.
DR   InParanoid; Q8C398; -.
DR   OMA; GLYVMQP; -.
DR   OrthoDB; 1202772at2759; -.
DR   PhylomeDB; Q8C398; -.
DR   TreeFam; TF314687; -.
DR   Reactome; R-MMU-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR   UniPathway; UPA00196; -.
DR   BioGRID-ORCS; 70325; 10 hits in 76 CRISPR screens.
DR   PRO; PR:Q8C398; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q8C398; protein.
DR   Bgee; ENSMUSG00000045140; Expressed in epiblast (generic) and 62 other tissues.
DR   ExpressionAtlas; Q8C398; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0032216; F:glucosaminyl-phosphatidylinositol O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR   InterPro; IPR009447; PIGW/GWT1.
DR   PANTHER; PTHR20661; PTHR20661; 1.
DR   Pfam; PF06423; GWT1; 1.
DR   PIRSF; PIRSF017321; GWT1; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Endoplasmic reticulum; Glycoprotein;
KW   GPI-anchor biosynthesis; Membrane; Phosphoprotein; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..503
FT                   /note="Phosphatidylinositol-glycan biosynthesis class W
FT                   protein"
FT                   /id="PRO_0000246283"
FT   TOPO_DOM        1..21
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        381..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        473..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         415
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z7B1"
FT   CARBOHYD        13
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   503 AA;  56841 MW;  3814E3D18680BACF CRC64;
     MSQKQLKEAF VRNLSGTSVL EVTQGLCFPA FCILCRGLWI IFSQHVCSFS NTWSTRFLMD
     FVVLIVPLVI TLTVLSSFIL LENLTVIVWG AWLLYQIYHR RTCYAKVPVQ KVFANFLKIS
     LESEYNPAIT CYRVINSVFT AIAILAVDFP LFPRRFAKTE LYGTGAMDFG VGGFIFGAAM
     VCPEVRRKSI EESRFNYLRK SLYSVWPLVF LGMGRLVIIK SIGYQEHSTE YGIHWNFFFT
     IIVVRLVTSL LLIIFPLNKS WIVAVSITVV YQLALDYTPL KRILLYGTDG SGTRVGFLNA
     NREGIISTLG YVTIHMAGVQ TGLYVLKGRA QVRDWIKATC WVFSVAVGFF ISLHIVQVNI
     EAVSRRMANL AFCLWVVASS LMLLSCLLLS GIILSFAQFL IKGSLVPCSW KLIQSPTTHK
     NHSESLILEA EKNQPSLCLI TALNRNQLFF FLLSNITTGL INLTMDTLHT GALWTLVVLS
     IYMFTNCLVI YVLDLQGKTI KFW
 
 
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