ID A0A026VYZ1_OOCBI Unreviewed; 2036 AA.
AC A0A026VYZ1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Voltage-dependent calcium channel type A subunit alpha-1 {ECO:0000313|EMBL:EZA48890.1};
DE Flags: Fragment;
GN ORFNames=X777_12932 {ECO:0000313|EMBL:EZA48890.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA48890.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA48890.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
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 EMBL; KK107566; EZA48890.1; -; Genomic_DNA.
DR STRING; 2015173.A0A026VYZ1; -.
DR EnsemblMetazoa; XM_026970487.1; XP_026826288.1; LOC105285138.
DR OMA; DPNKECA; -.
DR Proteomes; UP000053097; Unassembled WGS sequence.
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 GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 6.10.250.2500; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR InterPro; IPR011992; EF-hand-dom_pair.
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; 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:SF7; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR SMART; SM01062; Ca_chan_IQ; 1.
DR SUPFAM; SSF47473; EF-hand; 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, ECO:0000256|PIRSR:PIRSR602077-
KW 3}; 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:UP000053097};
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 88..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 528..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 620..643
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 691..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 825..843
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 863..883
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 892..910
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 959..981
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1073..1098
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1154..1172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1184..1207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1219..1243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1264..1293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1366..1390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1406..1441
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 431..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1645..1664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1714..1737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1753..1824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1838..1939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1997..2036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1684..1701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1893..1910
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1925..1939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2022..2036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 674
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1044
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EZA48890.1"
SQ SEQUENCE 2036 AA; 232778 MW; 96EA39A92C96868F CRC64;
RLAAAQEAAQ RDPGYARRRP RLAGLKTGLG DWTSFGGEVP GLVDMAPGRD QGGGAGGGGG
GGTTSLFILS EDNCIRKHTR FIIEWPPFEY AVLLTIIANC VVLALEEHLP HQDKTILAQK
LEATEVYFLG IFCVEASLKI LALGFVLHRG SYLRNIWNIM DFFVVVTGII TAFSQGIKRD
MDLRTLRAIR VLRPLKLVSG IPSLQVVLKS IIKAMAPLLQ IGLLVLFAIV IFAIIGLEFY
SGTLHKTCYN IEDINLIVRE GELPSPCNAN SDDEHPFGAH VCNANTSICL ERWEGPNSGI
TSFDNIGFAM LTVFQCITME GWTAILYWTN DALGSTYNWI YFIPLIVLGS FFMLNLVLGV
LSGEFAKERE KVENRQSFLK LRRQQQLERE LNSYLNWICK AEEVILAEER TTEEEKMHIL
EGRRRAAAKK KKLKNLGKSK STDTEEEEGE EDQDDGFSRA SYFKSKVKKQ GTCLQFWRAE
KRFRFWVRNS VKSQQFYWFV IILVFFNTIC VAVEHYGQPA WLTDFLFYAE FVFLALFMME
MFIKMYALGP RTYFESSFNR FDCIVISGSI FEVIWSALKS GSFGFSVLRA LRLLRIFKVT
KYWKSLRNLV ISLLSSMRSI ISLLFLLFLF ILIFALLGMQ LFGGQFNFSE GTPPTNFNTF
PIALLTVFQI LTGEDWNEVM YKGIESQNMA YSLYFIVLVL FGNYTLLNVF LAIAVDNLAN
AQELSAAEEE EKEEDKEKQL QELEKEIESL QKPGDGGAPK VEICPPSPTQ NFRDGRGETQ
TSEERRQDED DDTGPKPMLP YSSMFILSPT NPVRRAAHWI VNLRYFDFFI MVVISLSSIA
LAAEDPVSED APRNKILNYF DYAFTGVFTI EMVLKIIDLG IILHPGSYLR EFWNIMDAVV
VICAMVSFAF DMSGSSAGQN LSTIKSLRVL RVLRPLKTIK RVPKLKAVFD CVVNSLKNVI
NILIVYILFQ FIFAVIAVQL FNGRFFFCTD ESKYEPEECK GSFFVFEEGS SLPELKERKW
DLQSFHYDNV MVAMLTLFAV QTGEGWPQIL QNSMAATYED KGPIQNFRIE MSIFYIVYFI
VFPFFFVNIF VALIIITFQE QGEAELQDGE IDKNQKSCID FTIQARPLER YMPKERNSIK
YKIWRIVVST PFEYFIMILI VLNTLLLMMK FHQQTEQYKN TLKYMNMCFT GMFTIECILK
IAAFGVKNFF KDAWNTFDFI TVIGSIVDAL VIEFGENFIN VGFLRLFRAA RLIKLLRQGY
TIRILLWTFV QSFKALPYVC LLIAMLFFIY AIIGMQVFGN ISNNAETAID EHNNFQSFFA
GLMLLFRCAT GEAWPNIMLS CTKGKVCDEK ANKTAEDAND CGSNLAYVYF VSFIFFCSFL
MLNLFVAVIM DNFDYLTRDS SILGAHHLDE FVRIWAEYDP NATGKIHYTE MYDMLKNMDP
PLGFGNKCPN RLAYKKLIRM NMPVDGDGKV NFTTTLFALI RENLSIKMRC ADEMNQANDE
LRDTIRSIWP LQAKKMLDLL IPRNEELSRD KLTVGKIYVC LLILESWRST RFGQLKPAEQ
QSAFYNCLLD MAAVNHTGNN HGVGSRANSL EPVIRPDAKH ERHKEHRDED EGGALGVLAA
AEHRRQRSIR NKKVNWKMSH QYDILGSSGE SSQGGGGSGV VVNDEDRAPE LEPLLAEVPS
QRDDQNNYYH DHHHHDQYYD TDNDQYYDRH QYYHHHHHHH HDHHDHRPPS YYQHQKTYAP
RSSIRYHKEL QDVVPSDSRA GSVESLTHPD RILRPHHPSA PPHRRSRSPS IRRHSPTMPR
SPSPRRHGRY DHHGQYHEGP GFSDTVSNVV EIQRHIHQPH ASQYNHRHRI RGPWSASTSP
ARSPSPVHRI ERGGRYGTTS LEQRSRSPSP IGGGRPHHHH YRHHPHQHSY PVLVPRRGQG
RRLPPTPNKP STLQLKPTNI NFPKLNASPT HGHMAPAGPP HVGSMPGHVL QHPHPPHMPP
SMQPSHHPLS FEQAVAMGRS GRLLPSPVPN GYKPQPQSKQ RTPRSRHSDS DEDDWC
//
