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CRCM1_RAT
ID   CRCM1_RAT               Reviewed;         304 AA.
AC   Q5M848;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Calcium release-activated calcium channel protein 1;
DE   AltName: Full=Protein orai-1;
DE   AltName: Full=Transmembrane protein 142A;
GN   Name=Orai1; Synonyms=Cracm1, Tmem142a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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   [2]
RP   INTERACTION WITH CALM.
RX   PubMed=23109337; DOI=10.1074/jbc.m112.380964;
RA   Liu Y., Zheng X., Mueller G.A., Sobhany M., DeRose E.F., Zhang Y.,
RA   London R.E., Birnbaumer L.;
RT   "Crystal structure of calmodulin binding domain of orai1 in complex with
RT   Ca2+ calmodulin displays a unique binding mode.";
RL   J. Biol. Chem. 287:43030-43041(2012).
CC   -!- FUNCTION: Ca(2+) release-activated Ca(2+) (CRAC) channel subunit which
CC       mediates Ca(2+) influx following depletion of intracellular Ca(2+)
CC       stores and channel activation by the Ca(2+) sensor, STIM1. CRAC
CC       channels are the main pathway for Ca(2+) influx in T-cells and promote
CC       the immune response to pathogens by activating the transcription factor
CC       NFAT. Plays a prominent role in Ca(2+) influx at the basolateral
CC       membrane of mammary epithelial cells independently of the Ca(2+)
CC       content of endoplasmic reticulum or Golgi stores. May mediate
CC       transepithelial transport of large quantities of Ca(2+) for milk
CC       secretion. {ECO:0000250|UniProtKB:Q8BWG9,
CC       ECO:0000250|UniProtKB:Q96D31}.
CC   -!- ACTIVITY REGULATION: Oxidation at Cys-196 leads to inactivation of
CC       channel activity. {ECO:0000250|UniProtKB:Q96D31}.
CC   -!- SUBUNIT: Interacts with STIM1 and STIM2; this regulates channel
CC       activity (By similarity). Interacts with CALM; this may displace STIM1
CC       and STIM2 and might thereby modulate channel activity
CC       (PubMed:23109337). Interacts with CRACR2A/EFCAB4B; the interaction is
CC       direct and takes place in absence of Ca(2+) (By similarity). Forms a
CC       complex with CRACR2A/EFCAB4B and STIM1 at low concentration of Ca(2+),
CC       the complex dissociates at elevated Ca(2+) concentrations (By
CC       similarity). Interacts with SLC35G1 (By similarity). Interacts with
CC       UBQLN1 (By similarity). Interacts with ADCY8; interaction is calcium
CC       store depletion independent; interaction occurs in membrane raft;
CC       interaction increases markedly after store depletion; positively
CC       regulates SOCE-induced adenylate cyclase activity; contributes to the
CC       targeting of ADCY8 to discrete regions of the plasma membrane that are
CC       shielded from other calcium events (By similarity). Interacts with
CC       EFHB; the interaction takes place upon Ca(2+)-store depletion (By
CC       similarity). Interacts (via N- and C-termini) with ATP2C2 (via N-
CC       terminus); this interaction regulates Ca(2+) influx at the plasma
CC       membrane. {ECO:0000250|UniProtKB:Q8BWG9, ECO:0000250|UniProtKB:Q96D31,
CC       ECO:0000269|PubMed:23109337}.
CC   -!- INTERACTION:
CC       Q5M848; D4A5X1: Stim2; NbExp=3; IntAct=EBI-9700451, EBI-9700435;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96D31};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96D31}. Basolateral
CC       cell membrane {ECO:0000250|UniProtKB:Q8BWG9}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:Q96D31}. Note=Colocalizes with STIM1 at
CC       the cell membrane. {ECO:0000250|UniProtKB:Q96D31}.
CC   -!- PTM: N-glycosylated. N-glycosylation inhibits channel activity.
CC       {ECO:0000250|UniProtKB:Q96D31}.
CC   -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q96D31}.
CC   -!- PTM: Cys-196 is oxidated, leading to inactivation of channel activity.
CC       {ECO:0000250|UniProtKB:Q96D31}.
CC   -!- SIMILARITY: Belongs to the Orai family. {ECO:0000305}.
CC   -!- CAUTION: According to a report, ORAI1 has been shown to colocalize with
CC       UBQLN1 in the autophagosome as a target for autophagic degradation;
CC       ORAI1 is however not an autophagosomal protein.
CC       {ECO:0000250|UniProtKB:Q96D31}.
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DR   EMBL; BC088225; AAH88225.1; -; mRNA.
DR   RefSeq; NP_001014004.1; NM_001013982.1.
DR   AlphaFoldDB; Q5M848; -.
DR   BMRB; Q5M848; -.
DR   SMR; Q5M848; -.
DR   CORUM; Q5M848; -.
DR   IntAct; Q5M848; 2.
DR   STRING; 10116.ENSRNOP00000001806; -.
DR   BindingDB; Q5M848; -.
DR   ChEMBL; CHEMBL3721308; -.
DR   GlyGen; Q5M848; 1 site.
DR   PaxDb; Q5M848; -.
DR   GeneID; 304496; -.
DR   KEGG; rno:304496; -.
DR   UCSC; RGD:1311873; rat.
DR   CTD; 84876; -.
DR   RGD; 1311873; Orai1.
DR   eggNOG; KOG4298; Eukaryota.
DR   InParanoid; Q5M848; -.
DR   OrthoDB; 1197243at2759; -.
DR   PhylomeDB; Q5M848; -.
DR   PRO; PR:Q5M848; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR   GO; GO:0030426; C:growth cone; IDA:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0044853; C:plasma membrane raft; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0005262; F:calcium channel activity; ISO:RGD.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0015279; F:store-operated calcium channel activity; IMP:RGD.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0070509; P:calcium ion import; ISO:RGD.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; ISO:RGD.
DR   GO; GO:0061180; P:mammary gland epithelium development; ISO:RGD.
DR   GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISS:UniProtKB.
DR   GO; GO:0051928; P:positive regulation of calcium ion transport; ISS:UniProtKB.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISO:RGD.
DR   GO; GO:0002115; P:store-operated calcium entry; IMP:RGD.
DR   Gene3D; 1.20.140.140; -; 1.
DR   InterPro; IPR012446; CRAC_channel.
DR   InterPro; IPR038350; Orai_sf.
DR   PANTHER; PTHR31501; PTHR31501; 1.
DR   Pfam; PF07856; Orai-1; 1.
PE   1: Evidence at protein level;
KW   Adaptive immunity; Calcium; Calcium channel; Calcium transport;
KW   Calmodulin-binding; Cell membrane; Glycoprotein; Immunity; Ion channel;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN           1..304
FT                   /note="Calcium release-activated calcium channel protein 1"
FT                   /id="PRO_0000234383"
FT   TOPO_DOM        1..88
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        89..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..120
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..174
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        196..237
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..304
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          71..91
FT                   /note="Interaction with STIM1"
FT                   /evidence="ECO:0000250"
FT   REGION          275..295
FT                   /note="Interaction with STIM1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         298
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96D31"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   304 AA;  33040 MW;  98264D8880982C74 CRC64;
     MHPEPAPPPN NSNPELPLSG GSSTSGSRRS RRRSGDGEPT GAPPLPPPPA VSYPDWIGQS
     YSEVMSLNEH SMQALSWRKL YLSRAKLKAS SRTSALLSGF AMVAMVEVQL DTDHDYPPGL
     LIVFSACTTV LVAVHLFALM ISTCILPNIE AVSNVHNLNS VKESPHERMH RHIELAWAFS
     TVIGTLLFLA EVVLLCWVKF LPLKRQAGQP SPTKPPTEPA VVVANSSNNG GITPGEAAAI
     ASTAIMVPCG LVFIVFAVHF YRSLVSHKTD RQFQELNELA EFARLQDQLD HRGDHSLTPG
     THYA
 
 
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