ID A0A1S3F576_DIPOR Unreviewed; 2316 AA.
AC A0A1S3F576;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Voltage-dependent R-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=Cacna1e {ECO:0000313|RefSeq:XP_012870992.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012870992.1};
RN [1] {ECO:0000313|RefSeq:XP_012870992.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012870992.1};
RG RefSeq;
RL Submitted (NOV-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|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. {ECO:0000256|RuleBase:RU003808}.
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DR RefSeq; XP_012870992.1; XM_013015538.1.
DR STRING; 10020.ENSDORP00000001535; -.
DR GeneID; 105985130; -.
DR KEGG; dord:105985130; -.
DR CTD; 777; -.
DR InParanoid; A0A1S3F576; -.
DR OrthoDB; 1110761at2759; -.
DR Proteomes; UP000081671; 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; 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; 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.
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000081671};
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 93..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 503..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..625
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 680..703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1155..1174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1227..1246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1292..1314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1404..1429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1485..1503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1515..1538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1544..1562
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1609..1627
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1702..1726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1742..1777
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1961..2235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2265..2298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..2022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2023..2037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2068..2125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2126..2159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2193..2230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 657
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2316 AA; 261920 MW; C01F7FABC4CE5D6A CRC64;
MARFGEAVVG RPGSGDGDSD QSRNRQGTPV PASGPAAAYK QSKAQRARTM ALYNPIPVRQ
NCFTVNRSLF IFGEDNIVRK YAKKLIDWPP FEYMILATII ANCIVLALEQ HLPEDDKTPM
SRRLEKTEPY FIGIFCFEAG IKIVALGFIF HKGSYLRNGW NVMDFIVVLS GILATAGTHF
NTHVDLRTLR AVRVLRPLKL VSGIPSLQIV LKSIMKAMVP LLQIGLLLFF AILMFAIIGL
EFYSGKLHRA CFMNNSGILE GFDPPHPCGV QGCPAGYECK DWIGPNDGIT QFDNILFAVL
TVFQCITMEG WTTVLYNTND ALGATWNWLY FIPLIIIGSF FVLNLVLGVL SGEFAKERER
VENRRAFMKL RRQQQIEREL NGYRAWIDKA EEVMLAEENK NAGTSALEVL RRATIKRSRT
EAMTRDSSDE HCADISSVGT PLARASIKST KVDGASYFRH KERLLRISIR HMVKSQVFYW
IVLSLVALNT ACVAIVHHNQ PQWLTHLLYY AEFLFLGLFL LEMSLKMYGM GPRLYFHSSF
NCFDFGVTVG SIFEVVWAIF RPGTSFGISV LRALRLLRIF KITKYWASLR NLVVSLMSSM
KSIISLLFLL FLFIVVFALL GMQLFGGRFN FNDGTPSANF DTFPAAIMTV FQILTGEDWN
EVMYNGIRSQ GGVSSGMWSA IYFIVLTLFG NYTLLNVFLA IAVDNLANAQ ELTKDEQEEE
EAFNQKHALQ KAKEVSPMSA PNMPSMERDR RRRHHMSMWE PRSSHLRERR RRHHMSVWEQ
RTSQLRRHMQ MSSQEALNKE EAPPMNPLNP LNPLSPLNPL NAHPSLYRRS RPIEGLTLGL
GLEKCEEERI SRGGSLKGDG GGLSSALDNQ RSPLSLGKRE PPWLARPCHG NCDPTQQEAG
GGGETVVTFE DRARHRQSQR RSRHRRVRTE GKESSSASRS RSASQERSLD EVVPTEGEKE
HESRGSHGGK EPTIHEEERT QDLRRTNSLM VPRGSGLAEA LDEANTPLVM PQPELEVAKD
AVLTEQEQEG SSEQALLRDV QLDVGRGISQ SEPDLSCITA NTDKAATEST SVTVAIPDVG
PLVDSTVVHI SNKTDGEASP LKEAEIKEEE EEEVEKKKKK KERRETGKAM VPHSSMFIFS
TTNPIRRACH YIVNLRYFEM CILLVIAASS IALAAEDPVL TNSERNKVLR YFDYVFTGVF
TFEMVIKMID QGLILQDGSY FRDLWNILDF VVVVGALVAF ALANALGTNK GRDIKTIKSL
RVLRVLRPLK TIKRLPKLKA VFDCVVTSLK NVFNILIVYK LFMFIFAVIA VQLFKGKFFY
CTDSSKDTEK ECIGNYVDHE KNKMEVKGRE WKRHEFHYDN IIWALLTLFT VSTGEGWPQV
LQHSVDVTEE DRGPSRSNRM EMSIFYVVYF VVFPFFFVNI FVALIIITFQ EQGDKMMEEC
SLEKNERACI DFAISAKPLT RYMPQNRHTF QYRVWHFVVS PSFEYTIMAM IALNTVVLMM
KYYSAPCTYE LALKYLNIAF TMVFSLECVL KVIAFGFLNY FRDTWNIFDF ITVIGSITEI
ILTDSKLVNT SGFNMSFLKL FRAARLIKLL RQGYTIRILL WTFVQSFKAL PYVCLLIAML
FFIYAIIGMQ VFGNIKLDEE SHINRHNNFR SFFGSLMLLF RSATGEAWQE IMLSCLGEKG
CEPDTTAPSG QNENERCGTD LAYVYFVSFI FFCSFLMLNL FVAVIMDNFE YLTRDSSILG
PHHLDEFVRV WAEYDRAACG RIHYTEMYEM LTLMSPPLGL GKRCPSKVAY KRLVLMNMPV
AEDMTVHFTS TLMALIRTAL DIKIAKGGAD RQQLDSELQK ETLAIWPHLS QKMLDLLVPM
PKASDLTVGK IYAAMMIMDY YKQSKVKKQR QQLEEQKNAP MFQRMEPSSL PQEIIANAKS
LPYLQQDPVS GLSGRSGYPS MSPLSPQEIF QLACMDPADD GQFQEQQSLE PEVSELKSVQ
SSNHGIYLPS DTQEHTGSGR ASSMPRLTMD PQVVTDPSSM RRSFSTIRDK RSNSSWLEEF
SMERSSENTY KSRRRSYHSS LRLSAHRLNS DSGHKSDTHR SGGRERGRSK ERKHLLSPDV
SRCNSEERGN QGDWESPERR QSRSPSEGRS QTPNRQGTGS LSESSIPSIS DTSTPRRSRR
QLPPVPPKPR PLLSYSSLMR HAGSISPPAD GSEGGSPLTS QVRESSNACL TESSNSPHPQ
QGQHSSPQHY ISEPYLALHE DSHASDCGEE ETLTFEAAVA TSLGRSNTIG SAPPLRHSWQ
MPNGHYRRRR RGGPGPGMMC GAVSDLLSDT EEDDKC
//
