ID A0A2K6SGE7_SAIBB Unreviewed; 2120 AA.
AC A0A2K6SGE7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1B {ECO:0000313|Ensembl:ENSSBOP00000006460.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000006460.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000006460.1}
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. 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 Ensembl; ENSSBOT00000023195.1; ENSSBOP00000006460.1; ENSSBOG00000019548.1.
DR GeneTree; ENSGT00940000155275; -.
DR Proteomes; UP000233220; Unplaced.
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; 3.
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:UP000233220};
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 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 935..953
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 973..993
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1005..1023
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1066..1088
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1178..1203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1259..1277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1289..1312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1324..1348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1369..1398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1467..1490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1506..1541
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 607..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1698..1751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1763..1987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2101..2120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1698..1727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1829..1845
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1877..1901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1928..1987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2120 AA; 238292 MW; 591993F57A6C646B CRC64;
MKAMVPLLQI GLLLFFAILM FAIIGLEFYM GKFHKACFPN STDAEPVGDF PCGKEAPARL
CEGDTECREY WPGPNFGITN FDNILFAILT VFQCITMEGW TDILYNTNDA AGNTWNWLYF
IPLIIIGSFF MLNLVLGVLS GEFAKERERV ENRRAFLKLR RQQQIERELN GYLEWIFKAE
EVMLAEEDRN AEEKSPLDVL KRAATKKSRN DLIHAEEGED RFADLCAVGS PFARASLKSG
KTESSSYFRR KEKMFRFFIR RMVKAQSFYW VVLCVVALNT LCVAMVHYNQ PRRLTTALYF
AEFVFLGLFL TEMSLKMYGL GPRSYFRSSF NCFDFGVIVG SVFEVVWAAI KPGSSFGISV
LRALRLLRIF KVTKYWSSLR NLVVSLLNSM KSIISLLFLL FLFIVVFALL GMQLFGGQFN
FQDETPTTNF DTFPAAILTV FQILTGEDWN AVMYHGIESQ GGVSKGMFSS FYFIVLTLFG
NYTLLNVFLA IAVDNLANAQ ELTKDEEEME EAANQKLALQ KAKEVAEVSP MSAANISIAA
RQQNSAKARS VWEQRASQLR LQNLRASCEA LYSEMDPEER LRFATTRHLR PDMKTHLDRP
LVVELGRDGA RGTVGGKARP ETAEVPECAD PPRRHHRHRD KDRAPAAGDQ DRAEAPKVES
GEPGAREERP RPHRSHSKEA AGPPEARSER GRGPGPEGGR RHHRRGSPEE VAEREPRRHR
THRHQDPGKE GAGAKGERRA RHRGGPRTGP REAESGEEPA RRHRARHKAP PVHEAAEKEA
AEKEASEKEA EIVEADKEKE LRNHQPREPH CDLETSGTAT VGPVHTLPST CLQKVEEQPE
DADNQRNVTR MGSQPPDSST VVHIPVMLTG PSGEATVVPS GNVDLESQAE GKKEVEADDV
MRSGPRPIVP YSSMFCLSPT NLLRRFCHYI VTMRYFEMVI LVVIALSSIA LAAEDPVRTD
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 STRDQMQQAP GGLSQMGPVS LFHPLKATLE
QTQPAVLRGA RVFLRQKSST SLSNGGAIQN QESGIKESVS WGTQRTQDAP LEARPPLERG
HSTEIPVGQS GALAVDVQMQ SMTRRGPDGE PQPGLESQGR AASMPRLAAE TQPVADASPM
KRSISTLAQR PRGAHLCSTT PDRPPPSQAP HHHHHRCHRR KDRKQRSLEK GPSLSAETDG
APSSAAGPGL PLGEGPTGCK RERERRQERG RSQERRQPSS SSSEKQRFYS CDRFGGREPP
KPKPSLSSHP TSPTAGQEPG PHPQGSGSVN GSPLLSTSGA STPGRSGRRQ LPQTPLTPRP
SITYKTANSS PVHFAGAQTS LPAFSPGRLS RGLSEHNALL QRDPLSQPLA PGSRIGSDPY
LGQRLDSEAS VHALPEDTLT FEEAVATNSG RSSRTSYVSS LTSQSHPLRR VPNGYHCTLG
LSSGGRARHS YPHPDQDHWC
//
