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CACB2_BOVIN
ID   CACB2_BOVIN             Reviewed;         603 AA.
AC   Q9MZL5;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit beta-2;
DE            Short=CAB2;
DE   AltName: Full=Calcium channel voltage-dependent subunit beta 2;
GN   Name=CACNB2;
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 [MRNA].
RX   PubMed=10684870; DOI=10.1523/jneurosci.20-05-01685.2000;
RA   Cahill A.L., Hurley J.H., Fox A.P.;
RT   "Coexpression of cloned alpha(1B), beta(2a), and alpha(2)/delta subunits
RT   produces non-inactivating calcium currents similar to those found in bovine
RT   chromaffin cells.";
RL   J. Neurosci. 20:1685-1693(2000).
CC   -!- FUNCTION: The beta subunit of voltage-dependent calcium channels
CC       contributes to the function of the calcium channel by increasing peak
CC       calcium current, shifting the voltage dependencies of activation and
CC       inactivation, modulating G protein inhibition and controlling the
CC       alpha-1 subunit membrane targeting.
CC   -!- SUBUNIT: Component of a calcium channel complex consisting of a pore-
CC       forming alpha subunit (CACNA1S) and the ancillary subunits CACNB1 or
CC       CACNB2, CACNG1 and CACNA2D1. The channel complex contains alpha, beta,
CC       gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains either
CC       CACNB1 or CACNB2. Interacts with CACNA1C (By similarity). Interacts
CC       with RRAD. Interaction with RRAD regulates the trafficking of CACNA1C
CC       to the cell membrane. Interacts with TMIGD2 (By similarity). Interacts
CC       with CAMK2D. Interacts with CBARP (By similarity). Interacts with
CC       CAMK2A (By similarity). {ECO:0000250|UniProtKB:Q08289,
CC       ECO:0000250|UniProtKB:Q8VGC3}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- PTM: Regulated through phosphorylation at Thr-497 by CaMK2D.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AF174417; AAF26681.1; -; mRNA.
DR   RefSeq; NP_786983.1; NM_175789.2.
DR   AlphaFoldDB; Q9MZL5; -.
DR   SMR; Q9MZL5; -.
DR   ComplexPortal; CPX-3193; Cardiac muscle VGCC complex.
DR   IntAct; Q9MZL5; 2.
DR   STRING; 9913.ENSBTAP00000029344; -.
DR   BindingDB; Q9MZL5; -.
DR   PaxDb; Q9MZL5; -.
DR   PRIDE; Q9MZL5; -.
DR   Ensembl; ENSBTAT00000029344; ENSBTAP00000029344; ENSBTAG00000022000.
DR   GeneID; 327667; -.
DR   KEGG; bta:327667; -.
DR   CTD; 783; -.
DR   VEuPathDB; HostDB:ENSBTAG00000022000; -.
DR   VGNC; VGNC:26684; CACNB2.
DR   eggNOG; KOG3812; Eukaryota.
DR   GeneTree; ENSGT00950000182837; -.
DR   HOGENOM; CLU_021995_3_0_1; -.
DR   InParanoid; Q9MZL5; -.
DR   OrthoDB; 926074at2759; -.
DR   TreeFam; TF316195; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000022000; Expressed in cardiac ventricle and 103 other tissues.
DR   ExpressionAtlas; Q9MZL5; baseline and differential.
DR   GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IBA:GO_Central.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR   GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IBA:GO_Central.
DR   CDD; cd12040; SH3_CACNB2; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR035605; CACNB2_SH3.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR005444; VDCC_L_b2su.
DR   InterPro; IPR000584; VDCC_L_bsu.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF12052; VGCC_beta4Aa_N; 1.
DR   PRINTS; PR01626; LCACHANNELB.
DR   PRINTS; PR01628; LCACHANNELB2.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Calcium channel; Calcium transport; Cell membrane; Ion channel;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome; SH3 domain;
KW   Transport; Voltage-gated channel.
FT   CHAIN           1..603
FT                   /note="Voltage-dependent L-type calcium channel subunit
FT                   beta-2"
FT                   /id="PRO_0000144050"
FT   DOMAIN          59..128
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          135..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..603
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            492
FT                   /note="Required for CaMK2D-binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VGC3"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CC27"
FT   MOD_RES         163
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CC27"
FT   MOD_RES         493
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CC27"
FT   MOD_RES         497
FT                   /note="Phosphothreonine; by CaMK2D"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VGC3"
SQ   SEQUENCE   603 AA;  67842 MW;  217E10D1FA91B314 CRC64;
     MQCCGLVHRR RARVSYGSAD SYTSRPSDSD VSLEEDREAV RREAERQAQA QLEKAKTKPV
     AFAVRTNVSY SAAHEDDVPV PGMAISFEAK DFLHVKEKFN NDWWIGRLVK EGCEIGFIPS
     PVKLENMRLQ HEQRAKQGKF YSSKSGGNSS SSLGDIVPSS RKSTPPSSAI DIDATGLDAE
     DNDIPANHRS PKPSANSVTS PHSKEKRMPF FKKTEHTPPY DVVPSMRPVV LVGPSLKGYE
     VTDMMQKALF DFLKHRFEGR ISITRVTADI SLAKRSVLNN PSKHAIIERS NTRSSLAEVQ
     SEIERIFELA RTLQLVVLDA DTINHPAQLS KTSLAPIIVY VKISSPKVLQ RLIKSRGKSQ
     AKHLNVQMVA ADKLAQCPPE LFDVILDENQ LEDACEHLAD YLEAYWKATH PPSSSLPNPL
     LSRTLATSTL PVSPTLASNS QGSQGDQRTD RGAPGRSASQ AEEEHCPEPV KKAQHRSSTQ
     HHNHRSGTSR GLSRQETLDS ETQESRDSAY AEPKEEYSHE HADHYAPHRD HNHREEPHGG
     GEHRHREPRH RSRDPDREQD HNESNKQRSR HKSKDRYCDK DGEGLSRRRN EAADWNRDVY
     IRQ
 
 
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