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Database: UniProt
Entry: A0A096P4K9_PAPAN
LinkDB: A0A096P4K9_PAPAN
Original site: A0A096P4K9_PAPAN 
ID   A0A096P4K9_PAPAN        Unreviewed;      2095 AA.
AC   A0A096P4K9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-SEP-2017, entry version 19.
DE   RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1G {ECO:0000313|Ensembl:ENSPANP00000020284};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000020284, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000020284, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A.,
RA   Aqrawi P.A., Arias F.A., Attaway T.A., Awwad R.A., Babu C.B.,
RA   Bandaranaike D.B., Battles P.B., Bell A.B., Beltran B.B.,
RA   Berhane-Mersha D.B., Bess C.B., Bickham C.B., Bolden T.B.,
RA   Carter K.C., Chau D.C., Chavez A.C., Clerc-Blankenburg K.C.,
RA   Coyle M.C., Dao M.D., Davila M.L.D., Davy-Carroll L.D., Denson S.D.,
RA   Dinh H.D., Fernandez S.F., Fernando P.F., Forbes L.F., Francis C.F.,
RA   Francisco L.F., Fu Q.F., Garcia-Iii R.G., Garrett T.G., Gross S.G.,
RA   Gubbala S.G., Hirani K.H., Hogues M.H., Hollins B.H., Jackson L.J.,
RA   Javaid M.J., Jhangiani S.J., Johnson A.J., Johnson B.J., Jones J.J.,
RA   Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K., Kovar C.K.,
RA   Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P.,
RA   Perez Y.P., Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q.,
RA   Rouhana J.R., Ruiz M.R., Ruiz S.-J.R., Saada N.S., Santibanez J.S.,
RA   Scheel M.S., Schneider B.S., Simmons D.S., Sisson I.S., Tang L.-Y.T.,
RA   Thornton R.T., Tisius J.T., Toledanes G.T., Trejos Z.T., Usmani K.U.,
RA   Varghese R.V., Vattathil S.V., Vee V.V., Walker D.W.,
RA   Weissenberger G.W., White C.W., Williams A.W., Woodworth J.W.,
RA   Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N., Nazareth L.N.,
RA   Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000020284}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. This channel gives
CC       rise to T-type calcium currents. T-type calcium channels belong to
CC       the "low-voltage activated (LVA)" group and are strongly blocked
CC       by nickel and mibefradil. A particularity of this type of channels
CC       is an opening at quite negative potentials, and a voltage-
CC       dependent inactivation. T-type channels serve pacemaking functions
CC       in both central neurons and cardiac nodal cells and support
CC       calcium signaling in secretory cells and vascular smooth muscle.
CC       They may also be involved in the modulation of firing patterns of
CC       neurons which is important for information processing as well as
CC       in cell growth processes. {ECO:0000256|RuleBase:RU003808}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSPANP00000020284}.
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DR   EMBL; AHZZ01028109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHZZ01028110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSPANT00000018552; ENSPANP00000020284; ENSPANG00000022468.
DR   GeneTree; ENSGT00830000128242; -.
DR   Proteomes; UP000028761; Chromosome 16.
DR   ExpressionAtlas; A0A096P4K9; baseline.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0008332; F:low voltage-gated calcium channel activity; IEA:InterPro.
DR   GO; GO:0070509; P:calcium ion import; IEA:InterPro.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005445; VDCC_T_a1.
DR   InterPro; IPR030154; VDCC_T_a1G.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF256; PTHR10037:SF256; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01629; TVDCCALPHA1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU003808};
KW   Calcium channel {ECO:0000256|RuleBase:RU003808};
KW   Calcium transport {ECO:0000256|RuleBase:RU003808};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028761};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM     36     55       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    127    150       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    255    276       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    282    307       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    657    675       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    687    708       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    778    797       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    854    877       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1190   1208       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1228   1249       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1261   1280       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1325   1347       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1427   1450       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1514   1535       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1547   1570       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1648   1667       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1731   1753       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    318       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      656    882       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1188   1460       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1513   1763       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   COILED     1459   1493       {ECO:0000256|SAM:Coils}.
FT   COILED     1752   1776       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2095 AA;  233126 MW;  63061030436C5099 CRC64;
     MLVILLNCVT LGMFRPCEDI ACDSQRCRIL QAFDDFIFAF FAVEMVVKMV ALGIFGKKCY
     LGDTWNRLDF FIVIAGMLEY SLDLQNVSFS AVRTVRVLRP LRAINRVPSM RILVTLLLDT
     LPMLGNVLLL CFFVFFIFGI VGVQLWAGLL RNRCFLPENF SLPLSVDLER YYQTENEDES
     PFICSQPREN GMRSCRSVPT LRGEGGGGPP CGLDYEAYNS SSNTTCVNWN QYYTNCSAGE
     HNPFKGAINF DNIGYAWIAI FQVITLEGWV DIMYFVMDAH SFYNFIYFIL LIIVGSFFMI
     NLCLVVIATQ FSETKQRESQ LMREQRVRFL SNASTLASFS EPGSCYEELL KYLVYILRKA
     ARRLAQVSRA AGVRAGLLSS PAPLGGQETQ PSSSCSRSHR RLSVHHLVHH HHHHHHHYHL
     GNGTLRVPRA SPEIQDRDAN GSRRLMLPPP STPALSGGPP GGAESVHSFY HADCHLEPVR
     CQAPRPRSPS EASGRTVGSG KVYPTVHTSP PPETLKEKAL VEVAASSGPA TLTSLNIPPG
     PYSSMHKLLE TQSTGACQSS CKISSPCLKA DSGASGPDSC PYCARAGAGE VELADREMPD
     SDSEAVYEFT QDAQHSDLRD PHSWRPRSLG PDAEPSSVLA FWRLICDTFR KIVDSKYFGR
     GIMIAILVNT LSMGIEYHEQ PEELTNALEI SNIVFTSLFA LEMLLKLLVY GPFGYIKNPY
     NIFDGVIVVI SVWEIVGQQG GGLSVLRTFR LMRVLKLVRF LPALQRQLVV LMKTMDNVAT
     FCMLLMLFIF IFSILGMHLF GCKFASERDG DTLPDRKNFD SLLWAIVTVF QILTQEDWNK
     VLYNGMASTS SWAALYFIAL MTFGNYVLFN LLVAILVEGF QAEEISKRED ASGQLSCIQL
     PVDSQGGDAN KSESEPDFFS PSLDGDGDRK KCLALVSLGE HPELRKSLLP PLIIHTAATP
     MSLPKSTSTG LGEALGPTSR RTSSSGSAEP GAAHEMKSPP SARSSPHSPW SAASSWTSRR
     SSRNSLGRAP SLKRRSPSGE RRSLLSGEGQ ESQDEEESSE EERASPAGSD RRHRESLERE
     AKSSFDLPDT LQVPGLHRTA SGRGSASEHQ DCNGKSASGR LARALRPDDP PLDGDDADDE
     GNLSKGERVR AWIRARLPAC CLERDSWSAY IFPPQSRFRL LCHRIITHKM FDHVVLVIIF
     LNCITIAMER PKIDPHSAER IFLTLSNYIF TAVFLAEMTV KVVALGWCFG EQAYLRSSWN
     VLDGLLVLIS VIDILVSMVS DSGTKILGML RVLRLLRTLR PLRVISRAQG LKLVVETLMS
     SLKPIGNIVV ICCAFFIIFG ILGVQLFKGK FFVCQGEDTR NITNKSDCAE ASYRWVRHKY
     NFDNLGQALM SLFVLASKDG WVDIMYDGLD AVGVDQQPIM NHNPWMLLYF ISFLLIVAFF
     VLNMFVGVVV ENFHKCRQHQ EEEEARRREE KRLRRLEKKR RSKEKQMAEA QCKPYYSDYS
     RFRLLVHHLC TSHYLDLFIT GVIGLNVVTM AMEHYQQPQI LDEALKICNY IFTVIFVLES
     VFKLVAFGFR RFFQDRWNQL DLAIVLLSIM GITLEEIEVN ASLPINPTII RIMRVLRIAR
     VLKLLKMAVG MRALLDTVMQ ALPQVGNLGL LFMLLFFIFA ALGVELFGDL ECDETHPCEG
     LGRHATFRNF GMAFLTLFRV STGDNWNGIM KDTLRDCDQE STCYNTVISP IYFVSFVLTA
     QFVLVNVVIA VLMKHLEESN KEAKEEAELE AELELEMKTL SPQPHSPLGS PFLWPGVEGP
     DSPDSPKPGA LHPAAHARSA SHFSLEHPSD RQLFDTISLL IQGSLEWELK LMDELAGPGG
     QPSAFPSAPS LGGSDPQIPL AEMEALSLTS EIVSEPSCSL ALTDDSLPDD MHTLLLSAPE
     SNVQPHPTEL PGPDLLTVRK SGVSRTHSLP NDSYMCRHGS IAEGPLGHRG WGLPKAQSGS
     VLSVHSQPAD TSYILQLPKD APHLLQPYST PTWGTIPKLP PPGRSPLAQR PLRRQVSRCG
     KAGTGLGLDP LLLVMTRVDT FILPANIYCV PVMCQAQLQI PGTQYWAKQK RCVPS
//
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