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GRM2A_MOUSE
ID   GRM2A_MOUSE             Reviewed;         320 AA.
AC   Q3V3G7; B2RSP5; Q3V3E4;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=GRAM domain-containing protein 2A {ECO:0000305};
DE   AltName: Full=GRAM domain-containing protein 2;
GN   Name=Gramd2a {ECO:0000312|MGI:MGI:3528937}; Synonyms=Gramd2;
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=Thymus;
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 2).
RC   TISSUE=Brain;
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).
CC   -!- FUNCTION: Participates in the organization ofendoplasmic reticulum-
CC       plasma membrane contact sites (EPCS) with pleiotropic functions
CC       including STIM1 recruitment and calcium homeostasis. Constitutive
CC       tether that co-localize with ESYT2/3 tethers at endoplasmic reticulum-
CC       plasma membrane contact sites in a phosphatidylinositol lipid-dependent
CC       manner. Pre-marks the subset of phosphtidylinositol 4,5-biphosphate
CC       (PI(4,5)P2)-enriched EPCS destined for the store operated calcium entry
CC       pathway (SOCE). {ECO:0000250|UniProtKB:Q8IUY3}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q8IUY3}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q8IUY3}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q8IUY3}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q8IUY3}. Note=Localizes to endoplasmic
CC       reticulum-plasma membrane contact sites (EPCS). Anchored at the ER, PM
CC       binding is mediated via GRAM domain and phosphatidylinositol lipid
CC       interaction. Localizes to distinct EPCS than GRAMD1A.
CC       {ECO:0000250|UniProtKB:Q8IUY3}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3V3G7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3V3G7-2; Sequence=VSP_025478;
CC   -!- DOMAIN: GRAM domain is required for specific location to endoplasmic
CC       reticulum-plasma membrane contact sites (EPCS). Mediates interaction to
CC       phosphatidylinositol lipids and binding to plasma membrane.
CC       {ECO:0000250|UniProtKB:Q8IUY3}.
CC   -!- PTM: Phosphorylated.
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DR   EMBL; AK040545; BAE20581.1; -; mRNA.
DR   EMBL; AK041631; BAE20597.1; -; mRNA.
DR   EMBL; BC138948; AAI38949.1; -; mRNA.
DR   EMBL; BC138949; AAI38950.1; -; mRNA.
DR   CCDS; CCDS52818.1; -. [Q3V3G7-2]
DR   CCDS; CCDS90587.1; -. [Q3V3G7-1]
DR   RefSeq; NP_001028670.1; NM_001033498.1. [Q3V3G7-2]
DR   RefSeq; XP_006511336.1; XM_006511273.3.
DR   AlphaFoldDB; Q3V3G7; -.
DR   SMR; Q3V3G7; -.
DR   STRING; 10090.ENSMUSP00000096258; -.
DR   iPTMnet; Q3V3G7; -.
DR   PhosphoSitePlus; Q3V3G7; -.
DR   MaxQB; Q3V3G7; -.
DR   PaxDb; Q3V3G7; -.
DR   PRIDE; Q3V3G7; -.
DR   ProteomicsDB; 271332; -. [Q3V3G7-1]
DR   ProteomicsDB; 271333; -. [Q3V3G7-2]
DR   Antibodypedia; 26585; 65 antibodies from 17 providers.
DR   Ensembl; ENSMUST00000098661; ENSMUSP00000096258; ENSMUSG00000074259. [Q3V3G7-2]
DR   Ensembl; ENSMUST00000128944; ENSMUSP00000116879; ENSMUSG00000074259. [Q3V3G7-1]
DR   GeneID; 546134; -.
DR   KEGG; mmu:546134; -.
DR   UCSC; uc009pyk.1; mouse. [Q3V3G7-1]
DR   UCSC; uc009pyl.1; mouse. [Q3V3G7-2]
DR   CTD; 546134; -.
DR   MGI; MGI:3528937; Gramd2.
DR   VEuPathDB; HostDB:ENSMUSG00000074259; -.
DR   eggNOG; KOG1032; Eukaryota.
DR   GeneTree; ENSGT00940000159572; -.
DR   HOGENOM; CLU_050698_0_1_1; -.
DR   InParanoid; Q3V3G7; -.
DR   OMA; CSLNWDG; -.
DR   OrthoDB; 944155at2759; -.
DR   PhylomeDB; Q3V3G7; -.
DR   TreeFam; TF327695; -.
DR   BioGRID-ORCS; 546134; 0 hits in 73 CRISPR screens.
DR   ChiTaRS; Gramd2; mouse.
DR   PRO; PR:Q3V3G7; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q3V3G7; protein.
DR   Bgee; ENSMUSG00000074259; Expressed in layer of retina and 57 other tissues.
DR   ExpressionAtlas; Q3V3G7; baseline and differential.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0044232; C:organelle membrane contact site; ISS:UniProtKB.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; ISS:UniProtKB.
DR   GO; GO:2001256; P:regulation of store-operated calcium entry; ISS:UniProtKB.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR042624; RAMD2A.
DR   PANTHER; PTHR46973; PTHR46973; 2.
DR   Pfam; PF02893; GRAM; 1.
DR   SMART; SM00568; GRAM; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Endoplasmic reticulum; Lipid-binding;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..320
FT                   /note="GRAM domain-containing protein 2A"
FT                   /id="PRO_0000287455"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          74..141
FT                   /note="GRAM"
FT   REGION          33..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..14
FT                   /note="MQMKMMFFCLSDWQ -> MDTFPS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_025478"
SQ   SEQUENCE   320 AA;  36441 MW;  D13685B5D2BA330B CRC64;
     MQMKMMFFCL SDWQSNQQMH GKMAPLKSHV PCTEKPGKVQ EPPDDGSLHW SEGSKGEDIK
     KYSREGTLRS KYNQQYHKLF KDIPLEEVVL KVCSCALQRD LLLHGRLYIS PNWLCFHASL
     FGKDIKVVIP VVSVQLIKKH KMARLLPNGL AITTNTSQKY VFVSLLSRDS VYDMLRRVCT
     HLQPSSKKSL SIRKFPEEAE CESPEVLIPE MKWRKACSAP ASLSLPDSIS CISQIPTDST
     DSCFPSRKPP GSEAVCEKDA LEEEPSTDQE LRLWDSRLLK VIFVMICFLV LSSSYLAFRI
     SRLEQQLCSL SWGSPLPRDR
 
 
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