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Database: UniProt
Entry: G3QQ69_GORGO
LinkDB: G3QQ69_GORGO
Original site: G3QQ69_GORGO 
ID   G3QQ69_GORGO            Unreviewed;      2100 AA.
AC   G3QQ69;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1B {ECO:0000313|Ensembl:ENSGGOP00000004729.3};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000004729.3, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000004729.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000004729.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000004729.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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. This alpha-1B subunit gives rise to N-type
CC       calcium currents. N-type calcium channels belong to the 'high-voltage
CC       activated' (HVA) group. They are involved in pain signaling. Calcium
CC       channels containing alpha-1B subunit may play a role in directed
CC       migration of immature neurons. {ECO:0000256|RuleBase:RU003808}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. CACNA1B subfamily. {ECO:0000256|ARBA:ARBA00005685}.
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DR   EMBL; CABD030067536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030067537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030067538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030067539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030067540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030067541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030067542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030067543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030067544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030067545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSGGOT00000004851.3; ENSGGOP00000004729.3; ENSGGOG00000004807.3.
DR   eggNOG; KOG2301; Eukaryota.
DR   GeneTree; ENSGT00940000155275; -.
DR   HOGENOM; CLU_000540_1_0_1; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000001519; Chromosome 9.
DR   Bgee; ENSGGOG00000004807; Expressed in prefrontal cortex and 2 other cell types or tissues.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR002048; EF_hand_dom.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005447; VDCC_N_a1su.
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:SF6; VOLTAGE-DEPENDENT N-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1B; 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; PR01631; NVDCCALPHA1.
DR   SMART; SM01062; Ca_chan_IQ; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR   PROSITE; PS50222; EF_HAND_2; 1.
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};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
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        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        128..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        238..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        416..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        515..537
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        593..615
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        915..933
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        953..973
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        985..1003
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1046..1068
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1158..1183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1239..1257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1269..1292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1304..1328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1349..1378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1447..1470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1486..1521
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          655..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          817..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1678..1730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1743..1967
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..719
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..791
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..840
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1678..1707
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1776..1806
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1809..1825
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1857..1881
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1908..1967
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         219
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         569
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         1129
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ   SEQUENCE   2100 AA;  236077 MW;  278EB3BE1692003D CRC64;
     PFEYMILATI IANCIVLALE QHLPDGDKTP MSERLDDTEP YFIGIFCFEA GIKIIALGFV
     FHKGSYLRNG WNVMDFVVVL TGILATAGTD FDLRTLRAVR VLRPLKLVSG IPSLQVVLKS
     IMKAMVPLLQ IGLLLFFAIL MFAIIGLEFY MGKFHKACFP NSTDAEPVGD FPCGKEAPAR
     LCEGDTECRE YWPGPNFGIT NFDNILFAIL TVFQCITMEG WTDILYNTND AAGNTWNWLY
     FIPLIIIGSF FMLNLVLGVL SGEFAKERER VENRRAFLKL RRQQQIEREL NGYLEWIFKA
     EEVMLAEEDR NAEEKSPLDA VLKRAATKKS RNDLIHAEEG EDRFADLCAV GSPFARASLK
     SGKTESSSYF RRKEKMFRFF IRRMVKAQSF YWVVLCVVAL NTLCVAMVHY NQPRRLTTAL
     YFAEFVFLGL FLTEMSLKMY GLGPRSYFRS SFNCFDFGVI VGSVFEVVWA AIKPGSSFGI
     SVLRALRLLR IFKVTKYWSS LRNLVVSLLN SMKSIISLLF LLFLFIVVFA LLGMQLFGGQ
     FNFQDETPTT NFDTFPAAIL TVFQILTGED WNAVMYHGIE SQGGVSKGMF SSFYFIVLTL
     FGNYTLLNVF LAIAVDNLAN AQELTKDEEE MEEAANQKLA LQKAKEVAEV SPMSAANISI
     AAPPEARSER GRGPGPEGGR RHHRRGSPEE AAEREPRRHR AHRHQDPSKE CAGAKGERRA
     RHRGGPRAGP REAESGEEPA RRHRARHKAQ PAHEAVEKEA TEKEATEKEA EIVEADKEKE
     LRNHQPREPH CDLETSGTVT VGPMHTLPST CLQKVEEQPE DADNQRNVTR MGSQTPDPNT
     IVHIPVMLTG PPGEATVVPS GNVDLESQAE GKKEVEADDV MRSGPRPIVP YSSMFCLSPT
     NLLRRFCHYI VTMRYFEMVI LVVIALSSIA LAAEDPVHTD SPRNNALKYL DYIFTGVFTF
     EMVIKMIDLG LLLHPGAYFR DLWNILDFIV VSGALVAFAF SGSKGKDINT IKSLRVLRVL
     RPLKTIKRLP KLKAVFDCVV NSLKNVLNIL IVYMLFMFIF AVIAVQLFKG KFFYCTDESK
     ELERDCRGQY LDYEKEEVEA QPRQWKKYDF HYDNVLWALL TLFTVSTGEG WPMVLKHSVD
     ATYEEQGPSP GYRMELSIFY VVYFVVFPFF FVNIFVALII ITFQEQGDKV MSECSLEKNE
     RACIDFAISA KPLTRYMPQN RQSFQYKTWT FVVSPPFEYF IMAMIALNTV VLMMKFYDAP
     YEYELMLKCL NIVFTSMFSM ECVLKIIAFG VLNYFRDAWN VFDFVTVLGS ITDILVTEIA
     NNFINLSFLR LFRAARLIKL LRQGYTIRIL LWTFVQSFKA LPYVCLLIAM LFFIYAIIGM
     QVFGNIALDD DTSINRHNNF RTFLQALMLL FRSATGEAWH EIMLSCLSNQ ACDEQANATE
     CGSDFAYFYF VSFIFLCSFL MLNLFVAVIM DNFEYLTRDS SILGPHHLDE FIRVWAEYDP
     AACGRISYND MFEMLKHMSP PLGLGKKCPA RVAYKRLVRM NMPISNEDMT VHFTSTLMAL
     IRTALEIKLA PAGTKQHQCD AELRKEISVV WANLPQKTLD LLVPPHKPDE MTVGKVYAAL
     MIFDFYKQNK TTRDQMQQAP GGLSQMGPVS LFHPLKATLE QTQPAVLRGA RVFLRQKSST
     SLSNGGAIQN QESGIKESVS WGTQRTQDAP HEARPPLERG HSTEIPVGRS GALAVDVQMQ
     SITRRGPDGE PQPGLESQGR AASMPRLAAE TQPVTDASPM KRSISTLAQR PRGTHLCSTT
     PDRPPPSQAS HHHHHRCHRR RDRKQRSLEK GPSLSADMDG APSSAAGPGL APGEGPTGCR
     RERERRQERG RSQERRQPSS SSSEKQRFYS CDRFGGREPP KPKPSLSSHP TSPTAGQEPG
     PHPQGSGSVN GSPLLSTSGA STPGRGGRRQ LPQTPLTPRP SITYKTANSS PIHFAGAQTS
     LPAFSPGRLS RGLSEHNALL QRDPLSQPLA PGSRIGSDPY LGQRLDSEAS VHALPEDTLT
     FEEAVATNSG RSSRTSYVSS LTSQSHPLRR VPNGYHCTLG LSSGGRARHS YHHPDQDHWC
//
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