STIM1_BOVIN
ID STIM1_BOVIN Reviewed; 683 AA.
AC Q58CP9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Stromal interaction molecule 1;
DE Flags: Precursor;
GN Name=STIM1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Plays a role in mediating store-operated Ca(2+) entry (SOCE),
CC a Ca(2+) influx following depletion of intracellular Ca(2+) stores.
CC Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand
CC domain. Upon Ca(2+) depletion, translocates from the endoplasmic
CC reticulum to the plasma membrane where it activates the Ca(2+) release-
CC activated Ca(2+) (CRAC) channel subunit ORAI1. Involved in enamel
CC formation. Activated following interaction with STIMATE, leading to
CC promote STIM1 conformational switch. {ECO:0000250|UniProtKB:Q13586}.
CC -!- SUBUNIT: Monomer in the presence of Ca(2+). It oligomerizes in absence
CC of Ca(2+). Forms homooligomers and heterooligomers with STIM2.
CC Interacts (via the transmembrane region and the SOAR/CAD domain) with
CC SPPL3; the interaction promotes the binding of STIM1 to ORAI1.
CC Interacts with ORAI1. Interacts with MAPRE1; probably required for
CC targeting to the growing microtubule plus ends. Interacts with
CC CRACR2A/EFCAB4B; the interaction is direct and takes place in absence
CC of Ca(2+). Forms a complex with CRACR2A/EFCAB4B and ORAI1 at low
CC concentration of Ca(2+), the complex dissociates at elevated Ca(2+)
CC concentrations. Interacts with SARAF, promoting a slow inactivation of
CC STIM1-dependent SOCE activity, possibly by facilitating the
CC deoligomerization of STIM1 (By similarity). Interacts with EFHB; the
CC interaction takes place upon Ca(2+)-store depletion and inhibits the
CC association with SARAF (By similarity). Interacts with ASPH. Interacts
CC with SLC35G1; intracellular Ca(2+)-dependent. May interact with ATP1A1,
CC ATP2A2, ATP2B1, ATP2B4, KPNB1 and XPO1; through SLC35G1. Interacts with
CC TMEM203. Interacts with STIMATE, promoting STIM1 conformational switch
CC (By similarity). Interacts with TMEM178A (By similarity). Interacts
CC with CASQ1 (via C-terminal end and preferentially with the monomeric
CC form); this interaction increases in response to a depletion of
CC intracellular calcium, decreases both STIM1 aggregation and clustering,
CC interaction of STIM1 with ORAI1 and store-operated Ca(2+) entry (SOCE)
CC activity (By similarity). {ECO:0000250|UniProtKB:P70302,
CC ECO:0000250|UniProtKB:Q13586}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13586};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q13586}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q13586}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:Q13586}.
CC Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q13586}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q13586}. Note=Translocates from the
CC endoplasmic reticulum to the cell membrane in response to a depletion
CC of intracellular Ca(2+) and is detected at punctae corresponding to
CC junctions between the endoplasmic reticulum and the cell membrane.
CC Associated with the microtubule network at the growing distal tip of
CC microtubules. Colocalizes with ORAI1 at the cell membrane. Colocalizes
CC preferentially with CASQ1 at endoplasmic reticulum in response to a
CC depletion of intracellular calcium (By similarity).
CC {ECO:0000250|UniProtKB:Q13586}.
CC -!- DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates
CC interaction with MAPRE1 and targeting to the growing microtubule plus
CC ends. {ECO:0000250|UniProtKB:Q13586}.
CC -!- DOMAIN: The STIM1 Orai1-activating region/CRAC-activating domain
CC (SOAR/CAD) mediates interaction with ORAI1 to activate the channel.
CC {ECO:0000250|UniProtKB:Q13586}.
CC -!- PTM: Glycosylation is required for cell surface expression.
CC {ECO:0000250|UniProtKB:Q13586}.
CC -!- PTM: Phosphorylated predominantly on Ser residues.
CC {ECO:0000250|UniProtKB:Q13586}.
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DR EMBL; BT021898; AAX46745.1; -; mRNA.
DR RefSeq; NP_001030486.1; NM_001035409.1.
DR AlphaFoldDB; Q58CP9; -.
DR SMR; Q58CP9; -.
DR STRING; 9913.ENSBTAP00000017425; -.
DR iPTMnet; Q58CP9; -.
DR PaxDb; Q58CP9; -.
DR PeptideAtlas; Q58CP9; -.
DR PRIDE; Q58CP9; -.
DR GeneID; 534816; -.
DR KEGG; bta:534816; -.
DR CTD; 6786; -.
DR eggNOG; KOG4403; Eukaryota.
DR InParanoid; Q58CP9; -.
DR OrthoDB; 373308at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:AgBase.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:AgBase.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0044853; C:plasma membrane raft; ISS:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005246; F:calcium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:AgBase.
DR GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR GO; GO:0032237; P:activation of store-operated calcium channel activity; ISS:AgBase.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0005513; P:detection of calcium ion; ISS:AgBase.
DR GO; GO:0070166; P:enamel mineralization; ISS:UniProtKB.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISS:UniProtKB.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISS:AgBase.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; ISS:UniProtKB.
DR GO; GO:0002115; P:store-operated calcium entry; ISS:UniProtKB.
DR CDD; cd09573; SAM_STIM1; 1.
DR CDD; cd11722; SOAR; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR032393; SOAR.
DR InterPro; IPR037608; STIM.
DR InterPro; IPR037609; STIM1_SAM.
DR InterPro; IPR030463; STM1.
DR PANTHER; PTHR15136; PTHR15136; 1.
DR PANTHER; PTHR15136:SF9; PTHR15136:SF9; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF16533; SOAR; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Calcium; Calcium transport; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Endoplasmic reticulum; Glycoprotein; Ion transport; Membrane;
KW Metal-binding; Microtubule; Phosphoprotein; Reference proteome;
KW Sarcoplasmic reticulum; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..683
FT /note="Stromal interaction molecule 1"
FT /id="PRO_0000253465"
FT TOPO_DOM 23..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..683
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 61..96
FT /note="EF-hand"
FT DOMAIN 130..198
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 332..442
FT /note="SOAR/CAD"
FT /evidence="ECO:0000250"
FT REGION 488..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 246..440
FT /evidence="ECO:0000250"
FT MOTIF 640..643
FT /note="Microtubule tip localization signal"
FT COMPBIAS 488..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT MOD_RES 502
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P70302"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT MOD_RES 515
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70302"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT MOD_RES 663
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13586"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 683 AA; 77151 MW; 53938E436B093C69 CRC64;
MDVCARLALW LLWGLLLHHG QSLSQSHSEK ATGSGANSEE STAAEFCRID KPLCHSEDEK
LSFDAVRSIH KLMDDDANGD VDVEESDEFL REDLNYHDPT VKHSTFHGED KLISVEDLWK
AWKSSEVYNW TVDEVVQWLI TYVELPQYEE TFRKLQLSGH AMPRLAVTNT TMTGTVLKMT
DRSHRQKLQL KALDTVLFGP PLLTRHNHLK DFMLVVSIVI GVGGCWFAYI QNRYSKEHMK
KMMKDLEGLH RAEQSLHDLQ ERLHKAQEEH RTVEVEKVHL EKKLRDEINL AKQEAQRLKE
LREGTENERS RQKYAEEELE QVREALRKAE KELESHSSWY APEALQKWLQ LTHEVEVQYY
NIKKQNAEKQ LLVAKEGAEK IKKKRNTLFG TFHVAHSSSL DDVDHKILTA KQALSEVTAA
LRERLHRWQQ IEILCGFQIV NNPGIHSLVA ALNIDPSWMG STRPNPAHFI MTDDVDDMDE
EIVSPLSMQS PSLQSSVRQR LTEPQHGLGS QRDLTHSDSE SSLHMSDRQR LAPKPPQMIR
AADEALSAMT SNGSHRLIEG AHPGSLVEKL PDSPALAKKA LLALNHGLDK AHSLMELSSP
ALPSGSPHLD SSRSHSPSPP DPDTPSPAGD SRALQASRNT RIPHLAGKKA AAEEDNGSIG
EETDSSPGRK KFPLKIFKKP LKK
