ID A0A804HI37_HUMAN Unreviewed; 2168 AA. AC A0A804HI37; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 12-OCT-2022, entry version 5. DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808}; GN Name=CACNA1C {ECO:0000313|Ensembl:ENSP00000506882}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000506882, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000506882, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RG Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A., null.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000506882} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2021) 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. {ECO:0000256|RuleBase:RU003808}. CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma, T-tubule CC {ECO:0000256|ARBA:ARBA00024012}. Cell membrane, sarcolemma CC {ECO:0000256|ARBA:ARBA00004415}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004415}. Cell membrane CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004651}. Cell projection, dendrite CC {ECO:0000256|ARBA:ARBA00004279}. Membrane CC {ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU003808}. Perikaryon CC {ECO:0000256|ARBA:ARBA00004484}. Postsynaptic density membrane CC {ECO:0000256|ARBA:ARBA00034112}. CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC CC 1.A.1.11) family. CACNA1C subfamily. {ECO:0000256|ARBA:ARBA00024028}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC005293; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005342; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005344; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005414; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005866; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC006051; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455573; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455574; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_016875442.1; XM_017019953.1. DR SMR; A0A804HI37; -. DR PeptideAtlas; A0A804HI37; -. DR Ensembl; ENST00000683956.1; ENSP00000506882.1; ENSG00000151067.23. DR GeneID; 775; -. DR CTD; 775; -. DR HGNC; HGNC:1390; CACNA1C. DR GeneTree; ENSGT00940000156127; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; ENSG00000151067; Expressed in apex of heart and 100 other tissues. DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW. DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030315; C:T-tubule; IEA:UniProtKB-SubCell. DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro. DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW. DR Gene3D; 1.20.120.350; -; 4. DR InterPro; IPR031688; CAC1F_C. DR InterPro; IPR031649; GPHH_dom. DR InterPro; IPR005821; Ion_trans_dom. DR InterPro; IPR014873; VDCC_a1su_IQ. DR InterPro; IPR005451; VDCC_L_a1csu. DR InterPro; IPR005446; VDCC_L_a1su. DR InterPro; IPR002077; VDCCAlpha1. DR InterPro; IPR027359; Volt_channel_dom_sf. DR Pfam; PF08763; Ca_chan_IQ; 1. DR Pfam; PF16885; CAC1F_C; 2. DR Pfam; PF16905; GPHH; 1. DR Pfam; PF00520; Ion_trans; 4. DR PRINTS; PR00167; CACHANNEL. DR PRINTS; PR01630; LVDCCALPHA1. DR PRINTS; PR01635; LVDCCALPHA1C. DR SMART; SM01062; Ca_chan_IQ; 1. PE 1: Evidence at protein level; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU003808}; 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 Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Cell projection {ECO:0000256|ARBA:ARBA00023273}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Ion channel {ECO:0000256|RuleBase:RU003808}; 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 Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257}; KW Proteomics identification {ECO:0007829|MaxQB:A0A804HI37, KW ECO:0007829|PeptideAtlas:A0A804HI37}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Synapse {ECO:0000256|ARBA:ARBA00023018}; 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|RuleBase:RU003808}. FT TRANSMEM 158..175 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 195..215 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 227..245 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 298..320 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 379..400 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 412..434 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 555..572 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 592..615 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 684..703 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 756..783 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 926..948 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 968..989 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1047..1076 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1172..1199 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1250..1267 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1279..1301 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1313..1330 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1389..1412 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1482..1506 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1640..1674 FT /note="Ca_chan_IQ" FT /evidence="ECO:0000259|SMART:SM01062" FT REGION 103..128 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 479..511 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 794..891 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1760..1829 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1976..2010 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2133..2168 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 794..839 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1760..1805 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1979..1996 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2135..2159 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 2168 AA; 242681 MW; 7CD84435CCA5E1F3 CRC64; MLRAFVQPGT PAYQPLPSHL SANTEVKFKG TLVHEAQLNY FYISPGGSNY GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWQAAIDAAR QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK KQGSTTATRP PRALLCLTLK NPIRRACISI VEWKPFEIII LLTIFANCVA LAIYIPFPED DSNATNSNLE RVEYLFLIIF TVEAFLKVIA YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA ILEQATKADG ANALGGKGAG FDVKALRAFR VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH IALLVLFVII IYAIIGLELF MGKMHKTCYN QEGIADVPAE DDPSPCALET GHGRQCQNGT VCKPGWDGPK HGITNFDNFA FAMLTVFQCI TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI FGSFFVLNLV LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEDEGMDEEK PRNMSMPTSE TESVNTENVA GGDIEGENCG ARLAHRISKS KFSRYWRRWN RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT IASEHYNQPN WLTEVQDTAN KALLALFTAE MLLKMYSLGL QAYFVSLFNR FDCFVVCGGI LETILVETKI MSPLGISVLR CVRLLRIFKI TRYWNSLSNL VASLLNSVRS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF QILTGEDWNS VMYDGIMAYG GPSFPGMLVC IYFIILFICG NYILLNVFLA IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEL VEKPAVGESK EEKIELKSIT ADGESPPATK INMDDLQPNE NEDKSPYPNP ETTGEEDEEE PEMPVGPRPR PLSELHLKEK AVPMPEASAF FIFSSNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE DPVQHTSFRN HILGNADYVF TSIFTLEIIL KMTAYGAFLH KGSFCRNYFN ILDLLVVSVS LISFGIQSSA INVVKILRVL RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL FKGKLYTCSD SSKQTEAECK GNYITYKDGE VDHPIIQPRS WENSKFDFDN VLAAMMALFT VSTFEGWPEL LYRSIDSHTE DKGPIYNYRV EISIFFIIYI IIIAFFMMNI FVGFVIVTFQ EQGEQEYKNC ELDKNQRQCV EYALKARPLR RYIPKNQHQY KVWYVVNSTY FEYLMFVLIL LNTICLAMQH YGQSCLFKIA MNILNMLFTG LFTVEMILKL IAFKPKGYFS DPWNVFDFLI VIGSIIDVIL SETNPAEHTQ CSPSMNAEEN SRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIVML FFIYAVIGMQ VFGKIALNDT TEINRNNNFQ TFPQAVLLLF RCATGEAWQD IMLACMPGKK CAPESEPSNS TEGETPCGSS FAVFYFISFY MLCAFLIINL FVAVIMDNFD YLTRDWSILG PHHLDEFKRI WAEYDPEAKG RIKHLDVVTL LRRIQPPLGF GKLCPHRVAC KRLVSMNMPL NSDGTVMFNA TLFALVRTAL RIKTEGNLEQ ANEELRAIIK KIWKRTSMKL LDQVVPPAGD DEVTVGKFYA TFLIQEYFRK FKKRKEQGLV GKPSQRNALS LQAGLRTLHD IGPEIRRAIS GDLTAEEELD KAMKEAVSAA SEDDIFRRAG GLFGNHVSYY QSDGRSAFPQ TFTTQRPLHI NKAGSSQGDT ESPSHEKLVD STFTPSSYSS TGSNANINNA NNTALGRLPR PAGYPSTVST VEGHGPPLSP AIRVQEVAWK LSSNRCHSRE SQAAMAGQEE TSQDETYEVK MNHDTEACSE PSLLSTEMLS YQDDENRQLT LPEEDKRDIR QSPKRGFLRS ASLGRRASFH LECLKRQKDR GGDISQKTVL PLHLVHHQAL AVAGLSPLLQ RSHSPASFPR PFATPPATPG SRGWPPQPVP TLRLEGVESS EKLNSSFPSI HCGSWAETTP GGGGSSAARR VRPVSLMVPS QAGAPGRQFH GSASSLVEAV LISEGLGQFA QDPKFIEVTT QELADACDMT IEEMESAADN ILSGGAPQSP NGALLPFVNC RDAGQDRAGG EEDAGCVRAR GRPSEEELQD SRVYVSSL //