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Database: UniProt
Entry: A0A2K6JZG1_RHIBE
LinkDB: A0A2K6JZG1_RHIBE
Original site: A0A2K6JZG1_RHIBE 
ID   A0A2K6JZG1_RHIBE        Unreviewed;      2283 AA.
AC   A0A2K6JZG1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1A {ECO:0000313|Ensembl:ENSRBIP00000004389.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000004389.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000004389.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000004389.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC       of calcium ions into excitable cells and are also involved in a variety
CC       of calcium-dependent processes, including muscle contraction, hormone
CC       or neurotransmitter release, gene expression, cell motility, cell
CC       division and cell death. The isoform alpha-1A gives rise to P and/or Q-
CC       type calcium currents. {ECO:0000256|RuleBase:RU003808}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. CACNA1A subfamily. {ECO:0000256|ARBA:ARBA00037936}.
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DR   Ensembl; ENSRBIT00000022161.1; ENSRBIP00000004389.1; ENSRBIG00000018638.1.
DR   GeneTree; ENSGT00940000156518; -.
DR   OMA; KRMCQHR; -.
DR   Proteomes; UP000233180; Unplaced.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 4.
DR   Gene3D; 6.10.250.2180; -; 1.
DR   Gene3D; 6.10.250.2500; -; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR   InterPro; IPR005448; CACNA1A.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR45628; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR   PANTHER; PTHR45628:SF3; VOLTAGE-DEPENDENT P_Q-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1A; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01632; PQVDCCALPHA1.
DR   SMART; SM01062; Ca_chan_IQ; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR602077-1};
KW   Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW   ECO:0000256|RuleBase:RU003808};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU003808}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycoprotein {ECO:0000256|PIRSR:PIRSR602077-3};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602077-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW   ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM        38..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        235..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        385..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        511..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        587..611
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1107..1126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1146..1167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1179..1196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1241..1263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1353..1376
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1432..1453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1539..1557
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1635..1659
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1796..1830
FT                   /note="Voltage-dependent calcium channel alpha-1 subunit
FT                   IQ"
FT                   /evidence="ECO:0000259|SMART:SM01062"
FT   REGION          716..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          899..1086
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1837..1880
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1892..2283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          607..643
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        725..740
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..772
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..808
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        815..839
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..877
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        901..918
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        976..993
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1004..1026
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1057..1079
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1892..1915
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1946..1960
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1971..1990
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2041..2057
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2058..2094
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2095..2132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2145..2160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2266..2283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         216
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         565
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         1324
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ   SEQUENCE   2283 AA;  258496 MW;  80256E44594AA158 CRC64;
     MILATIIANC IVLALEQHLP DDDKTPMSER LDDTEPYFIG IFCFEAGIKI IALGFAFHKG
     SYLRNGWNVM DFVVVLTGIL ATVGTEFDLR TLRAVRVLRP LKLVSGIPSL QVVLKSIMKA
     MIPLLQIGLL LFFAILIFAI IGLEFYMGKF HTTCFEEGTD DIQGESPAPC GTEEPARTCP
     NGTKCQPYWE GPNNGITQFD NILFAVLTVF QCITMEGWTD LLYNSNDASG NTWNWLYFIP
     LIIIGSFFML NLVLGVLSGE FAKERERVEN RRAFLKLRRQ QQIERELNGY MEWISKAEEV
     ILAEDETDGE QRHPFDALRR TTIKKSKTDL LNPEEAEDQL ADIASVGSPF ARASIKSAKL
     ENSTFFHKKE RRMRFYIRRM VKTQAFYWTV LSLVALNTLC VAIVHYNQPE WLSDFLYYAE
     FIFLGLFMSE MFIKMYGLGT RPYFHSSFNC FDCGVIIGSI FEVIWAVIKP GTSFGISVLR
     ALRLLRIFKV TKYWASLRNL VVSLLNSMKS IISLLFLLFL FIVVFALLGM QLFGGQFNFD
     EGTPPTNFDT FPAAIMTVFQ ILTGEDWNEV MYDGIKSQGG VQGGMVFSIY FIVLTLFGNY
     TLLNVFLAIA VDNLANAQEL TKDEQEEEEA ANQKLALQKA KEVAEVSPLS AANMSIAVKE
     QQKNQKPAKS VWEQRTSEMR KQNLLASREA LYNEMDPDER WKAAYTRHLR PDMKTHLDRP
     LVVDPQENRN NNTNKSRAAE PTVDQRLGQQ RAEDFLRKQT RYHDRARDPS GSAGLDARRP
     WAGSQEAELS REGPYGRESD HHAREGSLEQ PGFWEGEVER GKAGDPHRRH VHRQGGSRES
     RSGSPRTGAD GEPRRHRTHR RPGEEGPEDK AERRVRHREG SRPLFILFHS LAFLRENQGS
     GVPVSGPNLS TTRPIQQDLG RQDPPLAEDI DNMKNNKLAT AESAGPHDSL GHAGLPQSPA
     KMGNSTDPGP TPAIPAMATN PQNAASRRMP NNPGNPSNPG PPKTPENSLI VTNPSGTQTN
     SAKTARKPDH TTVDIPPACP PPLNHTVVQV NKNANPDPLP KKEDEKKEEE EDDRGEDGPK
     PMPPYSSMFI LSTTNPLRRL CHYILNLRYF EMCILMVIAM SSIALAAEDP VQPNAPRNNV
     LRYFDYVFTG VFTFEMVIKM IDLGLVLHQG AYFRDLWNIL DFIVVSGALV AFAFTGNSKG
     KDINTIKSLR VLRVLRPLKT IKRLPKLKAV FDCVVNSLKN VFNILIVYML FMFIFAVVAV
     QLFKGKFFHC TDESKEFEKD CRGKYLLYEK NEVKARDREW KKYEFHYDNV LWALLTLFTV
     STGEGWPQVL KHSVDATFEN QGPSPGYRME MSIFYVVYFV VFPFFFVNIF VALIIITFQE
     QGDKMMEEYS LEKNERACID FAISAKPLTR HMPQNKQSFQ YRMWQFVVSP PFEYTIMAMI
     ALNTIVLMMK VSALHQPPAL LKPHLVPAST LNYFRDAWNI FDFVTVLGSI TDILVTEFGN
     NFINLSFLRL FRAARLIKLL RQGYTIRILL WTFVQSFKAL PYVCLLIAML FFIYAIIGMQ
     VFGNIGIDVE DEDSDEDEFQ ITEHNNFRTF FQALMLLFRS ATGEAWHNIM LSCLSGKPCD
     KNSGIQSREC GNEFAYFYFV SFIFLCSFLM LNLFVAVIMD NFEYLTRDSS ILGPHHLDEY
     VRVWAEYDPA AWGRMPYLDM YQMLRHMSPP LGLGKKCPAR VAYKRLLRMD LPVADDNTVH
     FNSTLMALIR TALDIKIAKG GADKQQMDAE LRKEMMAIWP NLSQKTLDLL VTPHKSTDLT
     VGKIYAAMMI MEYYRQSKAK KLQAMREEQD RTPLMFQRME PPSPTQEGGP GQNALPSAQL
     DPGGALMAHE SGLKESPSWV TQRAQEMFQK TGTWSPERGP PTDMPNSQPN SQSVEMREMG
     RDGYSDSEHY LPMEGQGRAA SMPRLPAENQ TISDTSPMKR SASVLGPKAR RLDDYSLERV
     PPEENQRHHQ RRRDRSHRTS ERSLGRYTDV DTGLGTDLSM TTQSGDLPSK ERDQERGRPK
     DRKHRQHHHH HHHHHPPPPD KDRYAQERPD HGRARARDQR WSRSPSEGRE HMAHRQGSSS
     VSGSPAPSTS GTSTPRRGRR QLPQTPSTPR PHVSYSPVIR KAGGSGPPQQ QQQQQAVARP
     GRAATSGPRR YPGPTAEPLA GDRPPMGGHS SGRSPRMERR VPGPARSESP RACRHGGARW
     PASGPQVSER TPRASGPACA SPSRHGRRLP NGYYPAHGLA RPRGPGSRKG LHEPYSESDD
     DWC
//
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