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PG2IP_MOUSE
ID   PG2IP_MOUSE             Reviewed;         699 AA.
AC   Q91YL7; Q8CBQ1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=PGAP2-interacting protein;
DE   AltName: Full=Cell wall biogenesis protein 43 C-terminal homolog;
GN   Name=Cwh43; Synonyms=Pgap2ip;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Urinary bladder;
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 MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH PGAP2/FRAG1, AND FUNCTION.
RX   PubMed=17761529; DOI=10.1091/mbc.e07-05-0482;
RA   Umemura M., Fujita M., Yoko-O T., Fukamizu A., Jigami Y.;
RT   "Saccharomyces cerevisiae CWH43 is involved in the remodeling of the lipid
RT   moiety of GPI anchors to ceramides.";
RL   Mol. Biol. Cell 18:4304-4316(2007).
CC   -!- FUNCTION: Involved in lipid remodeling during GPI-anchor maturation.
CC       {ECO:0000269|PubMed:17761529}.
CC   -!- SUBUNIT: Interacts with PGAP2/FRAG1. {ECO:0000269|PubMed:17761529}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91YL7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91YL7-2; Sequence=VSP_031684;
CC   -!- SIMILARITY: Belongs to the PGAP2IP family. {ECO:0000305}.
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DR   EMBL; AK035550; BAC29101.1; -; mRNA.
DR   EMBL; AK081976; BAC38385.1; -; mRNA.
DR   EMBL; BC016523; AAH16523.1; -; mRNA.
DR   CCDS; CCDS19341.1; -. [Q91YL7-1]
DR   RefSeq; NP_851840.1; NM_181323.2. [Q91YL7-1]
DR   AlphaFoldDB; Q91YL7; -.
DR   SMR; Q91YL7; -.
DR   IntAct; Q91YL7; 1.
DR   STRING; 10090.ENSMUSP00000031040; -.
DR   GlyGen; Q91YL7; 1 site.
DR   PhosphoSitePlus; Q91YL7; -.
DR   MaxQB; Q91YL7; -.
DR   PaxDb; Q91YL7; -.
DR   PRIDE; Q91YL7; -.
DR   ProteomicsDB; 288178; -. [Q91YL7-1]
DR   ProteomicsDB; 288179; -. [Q91YL7-2]
DR   Antibodypedia; 56515; 53 antibodies from 9 providers.
DR   DNASU; 231293; -.
DR   Ensembl; ENSMUST00000031040; ENSMUSP00000031040; ENSMUSG00000029154. [Q91YL7-1]
DR   Ensembl; ENSMUST00000065543; ENSMUSP00000069563; ENSMUSG00000029154. [Q91YL7-2]
DR   GeneID; 231293; -.
DR   KEGG; mmu:231293; -.
DR   UCSC; uc008xsx.1; mouse. [Q91YL7-1]
DR   UCSC; uc012dxc.1; mouse. [Q91YL7-2]
DR   CTD; 80157; -.
DR   MGI; MGI:2444131; Cwh43.
DR   VEuPathDB; HostDB:ENSMUSG00000029154; -.
DR   eggNOG; ENOG502QVQN; Eukaryota.
DR   GeneTree; ENSGT00510000048509; -.
DR   HOGENOM; CLU_009808_1_0_1; -.
DR   InParanoid; Q91YL7; -.
DR   OMA; ITAGIWT; -.
DR   OrthoDB; 581809at2759; -.
DR   PhylomeDB; Q91YL7; -.
DR   TreeFam; TF328857; -.
DR   BioGRID-ORCS; 231293; 4 hits in 74 CRISPR screens.
DR   ChiTaRS; Cwh43; mouse.
DR   PRO; PR:Q91YL7; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q91YL7; protein.
DR   Bgee; ENSMUSG00000029154; Expressed in pyloric antrum and 65 other tissues.
DR   Genevisible; Q91YL7; MM.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.60.10.10; -; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR027317; PGAP2IP.
DR   PANTHER; PTHR14859:SF1; PTHR14859:SF1; 1.
DR   SUPFAM; SSF56219; SSF56219; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..699
FT                   /note="PGAP2-interacting protein"
FT                   /id="PRO_0000320616"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          607..627
FT                   /note="Required for function in lipid remodeling"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        536
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         268..353
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031684"
SQ   SEQUENCE   699 AA;  78180 MW;  4F41975D6570D5F8 CRC64;
     MPGLWRAIAL ETLLGYVSWS LYHGLSPMIY YFPLQTLELT GLEFFCVAFL SPILLTIPPL
     WKLVNKKWTL SLLRIVTVGS IASFEAPNAK LRLMVLALGV SSSLIVQTVT WWSGSGLQRY
     LKIWGFILGH VLLLVLRIWY TSLNPIWSYQ MSNRVILTLS AVAVLDRIGT DGDYRNPEGK
     KPREVATGRT SLSSWLLPGA AFGSLLFLTH WIFGEVSIVS RWAVSGHPHP GPDPNPFGGA
     VLLGFSSGLM LSGSSWLHDA GLAWWMTGAA SAMGLLYLRT WAAAVSGCVL AVFTGSMWPQ
     VLGHLVNSGK NSGEAMATGM ILYVLQTFFC AWCTAFKFVP GGVYARERSD VLLGTIMVII
     GLSMLFGPKK NLDFLLQTKN SPKTLLRCSE KYMKLILWLF VGVGLLGLGL RHRTYERQLG
     RGAPATVVSA AIWPFRFGYD NEGWPNLERS AQLLKETGAD FITILESDAS KPYIGNNDLT
     MWLGEKLGFY TDFGPSTRDH TWGIMVLSRY PIVRSEHHLL PSPEGEIAPA ITMTVNVSNR
     LVDFVVTHFG NHEDDLDRKL QAIAVSKLLK NCSNQVIFLG YITSEPGSRD YIQLTKHGNV
     KDIDSSDGDR WCEYIMYRGL IRLGYARISH AELSDSEIQM AKFRIPDDPA NYRDNQKVVI
     DHRGVPKNIH FNPRFGSYKE GHNYENTHHF HMNTPKYFV
 
 
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