ID A0A2R8ZZW4_PANPA Unreviewed; 2236 AA.
AC A0A2R8ZZW4;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Voltage-dependent R-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1E {ECO:0000313|Ensembl:ENSPPAP00000010133.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000010133.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000010133.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000010133.1}
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-1E gives rise to R-type
CC calcium currents. {ECO:0000256|RuleBase:RU003808}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
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DR EMBL; AJFE02087282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02087283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02087284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPPAT00000032780.1; ENSPPAP00000010133.1; ENSPPAG00000027818.1.
DR GeneTree; ENSGT00940000155601; -.
DR OMA; XRERRRR; -.
DR Proteomes; UP000240080; Chromosome 1.
DR Bgee; ENSPPAG00000027818; 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: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; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR005449; VDCC_R_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:SF5; VOLTAGE-DEPENDENT R-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1E; 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; PR01633; RVDCCALPHA1.
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000240080};
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 81..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 492..510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 592..614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 669..692
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1122..1141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1194..1211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1255..1277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1367..1392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1448..1466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1478..1501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1507..1525
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1572..1590
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1665..1689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1826..1860
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1984..2093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2129..2148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2186..2219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 688..715
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1988..2045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2046..2079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2236 AA; 252988 MW; F8FE9B96A70AA89D CRC64;
MARFGEAVVA RPGSGDGDSD QSRNRQGTPV PASGQAAAYK QTKAQRARTM ALYNPIPVRQ
NCFTVNRSLF IFGEDNIVRK YYMILATIIA NCIVLALEQH LPEDDKTPMS RRLEKTEPYF
IGIFCFEAGI KIVALGFIFH KGSYLRNGWN VMDFIVVLSG ILATAGTHFN THVDLRTLRA
VRVLRPLKLV SGIPSLQIVL KSIMKAMVPL LQIGLLLFFA ILMFAIIGLE FYSGKLHRAC
FMNNSGILEG FDPPHPCGVQ GCPAGYECKD WIGPNDGITQ FDNILFAVLT VFQCITMEGW
TTVLYNTNDA LGATWNWLYF IPLIIIGSFF VLNLVLGVLS GEFAKERERV ENRRAFMKLR
RQQQIERELN GYRAWIDKAE EVMLAEENKN AGTSALEVLR RATIKRSRTE AMTRDSSDEH
CVDISSVGTP LARASIKSAK VDGVSYFRHK ERLLRISIRH MVKSQVFYWI VLSLVALNTA
CVAIVHHNQP QWLTHLLYYA EFLFLGLFLL EMSLKMYGMG PRLYFHSSFN CFDFGVTVGS
IFEVVWAIFR PGTSFGISVL RALRLLRIFK ITKYWASLRN LVVSLMSSMK SIISLLFLLF
LFIVVFALLG MQLFGGRFNF NDGTPSANFD TFPAAIMTVF QILTGEDWNE VMYNGIRSQG
GVSSGMWSAI YFIVLTLFGN YTLLNVFLAI AVDNLANAQE LTKDEQEEEE AFNQKHALQK
AKEVSPMSAP NMPSIERERR RRHHMSVWEQ RTSQLRKHMQ MSSQEALNRE EAPTMNPLNP
LNPLSSLNPL NAHPSLYRRP RAIEGLALGL ALEKFEEERI SRGGSLKGDG GDRSSALDNQ
RTPLSLGQRE PPWLARPCHG NCDPTQQEAG GGEAVVTFED RARHRQSQRR SRHRRVRTEG
KESSSASRSR SASQERSLDE AMPTEGEKDH ELRGNHGAKE PTIQEERAQD LRRTNSLMVS
RGSRLAGGLD EADTPLVLPH PELEVGKHVV LTEQEPEGSS EQALLGNVQL DMGRVISQSE
PDLSCITANT DKATTESTSV TVAIPDVDPL VDSTVVHISN KTDGEASPLK EAEIREDEEE
VEKKKQKKEK RETGKAMVPH SSMFIFSTTN PIRRACHYIV NLRYFEMCIL LVIAASSIAL
AAEDPVLTNS ERNKVLRYFD YVFTGVFTFE MVIKMIDQGL ILQDGSYFRD LWNILDFVVV
VGALVAFALA TNKGRDIKTI KSLRVLRVLR PLKTIKRLPK LKAVFDCVVT SLKNVFNILI
VYKLFMFIFA VIAVQLFKGK FFYCTDSSKD TEKECIGNYV DHEKNKMEVK GREWKRHEFH
YDNIIWALLT LFTVSTGEGW PQVLQHSVDV TEEDRGPSRS NRMEMSIFYV VYFVVFPFFF
VNIFVALIII TFQEQGDKMM EECSLEKNER ACIDFAISAK PLTRYMPQNR HTFQYRVWHF
VVSPSFEYTI MAMIALNTVV LMMKYYSAPC TYELALKYLN IAFTMVFSLE CVLKVIAFGF
LNYFRDTWNI FDFITVIGSI TEIILTDSKL VNTSGFNMSF LKLFRAARLI KLLRQGYTIR
ILLWTFVQSF KALPYVCLLI AMLFFIYAII GMQVFGNIKL DEESHINRHN NFRSFFGSLM
LLFRSATGEA WQEIMLSCLG EKGCEPDTTA PSGQNENERC GTDLAYVYFV SFIFFCSFLM
LNLFVAVIMD NFEYLTRDSS ILGPHHLDEF VRVWAEYDRA ACGRIPYKDM YKLVRVISPP
LGLGENCPYR VACKRLVLMN MPVAEDMTVH FTSTLMALIR TALDIKIAKG GADRQQLDSE
LQKETLAIWP HLSQKMLDLL VPMPKASDLT VGKIYAAMMI MDYYKQSKVK KQRQQLEEQK
NAPMFQRMEP SSLPQEIIAN AKALPYLQQD PVSGLSGRSG YPSMSPLSPQ DIFQLACMDP
ADDGQFQERQ SLVVTDPSSM RRSFSTIRDK RSNSSWLEEF SMERSSENTY KSRRRSYHSS
LRLSAHRLNS DSGHKSDTHR SGGRERGRSK ERKHLLSPDV SRCNSEERGT QADWESPERR
QSRSPSEGRS QTPNRQGTGS LSESSIPSVS DTSTPRRSRR QLPPVPPKPR PLLSYSSLIR
HAGSISPPAD GSEEGSPLTS QALESNNACL TESSNSPHPQ QSQHASPQRY ISEPYLALHE
DSHASDCGEE ETLTFEAAVA TSLGRSNTIG SAPPLRHSWQ MPNGHYRRRR RGGPGPGMMC
GAVNNLLSDT EEDDKC
//