CACB1_RABIT
ID CACB1_RABIT Reviewed; 524 AA.
AC P19517;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit beta-1;
DE Short=CAB1;
DE AltName: Full=Calcium channel voltage-dependent subunit beta 1;
GN Name=CACNB1; Synonyms=CACNLB1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Skeletal muscle;
RX PubMed=2549640; DOI=10.1126/science.2549640;
RA Ruth P., Roehrkasten A., Biel M., Bosse E., Regulla S., Meyer H.E.,
RA Flockerzi V., Hoffmann F.;
RT "Primary structure of the beta subunit of the DHP-sensitive calcium channel
RT from skeletal muscle.";
RL Science 245:1115-1118(1989).
RN [2]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH CACNA1A;
RP CACNA1B; CACNA1C AND CACNA1S.
RX PubMed=7509046; DOI=10.1038/368067a0;
RA Pragnell M., de Waard M., Mori Y., Tanabe T., Snutch T.P., Campbell K.P.;
RT "Calcium channel beta-subunit binds to a conserved motif in the I-II
RT cytoplasmic linker of the alpha 1-subunit.";
RL Nature 368:67-70(1994).
RN [3]
RP SUBUNIT.
RX PubMed=21127204; DOI=10.1096/fj.10-172353;
RA Yang L., Katchman A., Morrow J.P., Doshi D., Marx S.O.;
RT "Cardiac L-type calcium channel (Cav1.2) associates with gamma subunits.";
RL FASEB J. 25:928-936(2011).
RN [4] {ECO:0007744|PDB:5GJV, ECO:0007744|PDB:5GJW}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 80-174 AND 265-463,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=27580036; DOI=10.1038/nature19321;
RA Wu J., Yan Z., Li Z., Qian X., Lu S., Dong M., Zhou Q., Yan N.;
RT "Structure of the voltage-gated calcium channel Ca(v)1.1 at 3.6A
RT resolution.";
RL Nature 537:191-196(2016).
CC -!- FUNCTION: Regulatory subunit of L-type calcium channels
CC (PubMed:7509046). Regulates the activity of L-type calcium channels
CC that contain CACNA1A as pore-forming subunit (PubMed:7509046).
CC Regulates the activity of L-type calcium channels that contain CACNA1C
CC as pore-forming subunit and increases the presence of the channel
CC complex at the cell membrane. Required for functional expression L-type
CC calcium channels that contain CACNA1D as pore-forming subunit.
CC Regulates the activity of L-type calcium channels that contain CACNA1B
CC as pore-forming subunit (By similarity). {ECO:0000250|UniProtKB:Q02641,
CC ECO:0000269|PubMed:7509046}.
CC -!- SUBUNIT: Regulatory subunit of L-type calcium channels that consist of
CC a pore-forming alpha subunit and auxiliary beta, gamma and delta
CC subunits (PubMed:7509046, PubMed:27580036). Interacts with CACNA1A,
CC CACNA1B, CACNA1C and CACNA1S (PubMed:7509046). Component of a calcium
CC channel complex consisting of a pore-forming alpha subunit (CACNA1S)
CC and the ancillary subunits CACNB1 or CACNB2, CACNG1 and CACNA2D1
CC (PubMed:27580036). Identified in a complex with CACNA1C
CC (PubMed:7509046, PubMed:21127204). Identified in a complex with the L-
CC type calcium channel subunits CACNA1C, CACNA2D1, CACNB1 and one of the
CC gamma subunits (CACNG4, CACNG6, CACNG7, or CACNG8) (PubMed:21127204).
CC Part of a L-type calcium channel complex that contains CACNA1D,
CC CACNA2D1 and CACNB1. Part of a L-type calcium channel complex that
CC contains CACNA1B, CACNA2D1 and CACNB1 (By similarity). Interacts with
CC JSRP1. Interacts with RYR1 (By similarity). Interacts with CBARP (By
CC similarity). {ECO:0000250|UniProtKB:P54283,
CC ECO:0000250|UniProtKB:Q02641, ECO:0000250|UniProtKB:Q8R3Z5,
CC ECO:0000269|PubMed:21127204, ECO:0000269|PubMed:27580036,
CC ECO:0000269|PubMed:7509046}.
CC -!- INTERACTION:
CC P19517; P07293: CACNA1S; NbExp=4; IntAct=EBI-978604, EBI-8613624;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:27580036, ECO:0000305|PubMed:7509046}; Peripheral
CC membrane protein {ECO:0000269|PubMed:27580036,
CC ECO:0000305|PubMed:7509046}; Cytoplasmic side
CC {ECO:0000269|PubMed:27580036, ECO:0000305|PubMed:7509046}. Cell
CC membrane {ECO:0000250|UniProtKB:Q02641}; Peripheral membrane protein
CC {ECO:0000269|PubMed:27580036, ECO:0000305|PubMed:7509046}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
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DR EMBL; M25817; AAA31180.1; -; mRNA.
DR EMBL; M25514; AAA56855.1; -; mRNA.
DR PIR; A41347; A41347.
DR RefSeq; NP_001075748.1; NM_001082279.1.
DR PDB; 5GJV; EM; 3.60 A; B=80-174, C=265-463.
DR PDB; 5GJW; EM; 3.90 A; B=80-174, C=265-463.
DR PDB; 6JP5; EM; 2.90 A; B/C=80-524.
DR PDB; 6JP8; EM; 2.70 A; B/C=80-524.
DR PDBsum; 5GJV; -.
DR PDBsum; 5GJW; -.
DR PDBsum; 6JP5; -.
DR PDBsum; 6JP8; -.
DR AlphaFoldDB; P19517; -.
DR SMR; P19517; -.
DR BioGRID; 1172132; 2.
DR ComplexPortal; CPX-3189; Skeletal muscle VGCC complex.
DR DIP; DIP-37525N; -.
DR IntAct; P19517; 2.
DR STRING; 9986.ENSOCUP00000005545; -.
DR iPTMnet; P19517; -.
DR GeneID; 100009109; -.
DR KEGG; ocu:100009109; -.
DR CTD; 782; -.
DR eggNOG; KOG3812; Eukaryota.
DR InParanoid; P19517; -.
DR OrthoDB; 926074at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:UniProtKB.
DR GO; GO:0030315; C:T-tubule; IDA:UniProtKB.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IC:ComplexPortal.
DR GO; GO:0045933; P:positive regulation of muscle contraction; IC:ComplexPortal.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
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; IPR005443; VDCC_L_b1su.
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; PR01627; LCACHANNELB1.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Direct protein sequencing; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; SH3 domain; Transport;
KW Voltage-gated channel.
FT CHAIN 1..524
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-1"
FT /id="PRO_0000144048"
FT DOMAIN 100..169
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54283"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54283"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54283"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R3Z5"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54283"
FT CONFLICT 304
FT /note="L -> R (in Ref. 1; AAA56855)"
FT /evidence="ECO:0000305"
FT HELIX 80..94
FT /evidence="ECO:0007829|PDB:6JP8"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6JP8"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:6JP8"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:6JP8"
FT STRAND 141..151
FT /evidence="ECO:0007829|PDB:6JP8"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:6JP8"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:6JP8"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:6JP8"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:6JP8"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 288..303
FT /evidence="ECO:0007829|PDB:6JP8"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:6JP8"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 344..356
FT /evidence="ECO:0007829|PDB:6JP8"
FT TURN 357..361
FT /evidence="ECO:0007829|PDB:6JP8"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:6JP8"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:6JP8"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 394..401
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 412..424
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:6JP8"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 439..457
FT /evidence="ECO:0007829|PDB:6JP8"
SQ SEQUENCE 524 AA; 57825 MW; 629420640A7457CC CRC64;
MVQKTSMSRG PYPPSQEIPM EVFDPSPQGK YSKRKGRFKR SDGSTSSDTT SNSFVRQGSA
ESYTSRPSDS DVSLEEDREA LRKEAERQAL AQLEKAKTKP VAFAVRTNVG YNPSPGDEVP
VEGVAITFEP KDFLHIKEKY NNDWWIGRLV KEGCEVGFIP SPVKLDSLRL LQEQKLRQSR
LSSSKSGDNS SSSLGDVVTG TRRPTPPASG NEMTNLAFEL EPLDLEEDEA ELGEQSGSAK
TSVSSVTTPP PHGTRIPFFK KTEHVPPYDV VPSMRPIILV GPSLKGYEVT DMMQKALFDF
LKHLFDGRIS ITRVTADISL AKRSVLNNPS KHIIIERSNT RSSLAEVQSE IERIFELART
LQLVALDADT INHPAQLSKT SLAPIIVYIK ITSPKVLQRL IKSRGKSQSK HLNVQIAASE
KLAQCPPEMF DIILDENQLE DACEHLAEYL EAYWKATHPP SSTPPNPLLN RTMATAALAA
SPAPVSNLQV QVLTSLRRNL SFWGGLETSQ RGGGAVPQQQ EHAM
