ID A0A2Y9D6K0_TRIMA Unreviewed; 2179 AA.
AC A0A2Y9D6K0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=LOC101357085 {ECO:0000313|RefSeq:XP_004368677.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004368677.1};
RN [1] {ECO:0000313|RefSeq:XP_004368677.1}
RP IDENTIFICATION.
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. {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. CACNA1D subfamily. {ECO:0000256|ARBA:ARBA00010354}.
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DR RefSeq; XP_004368677.1; XM_004368620.1.
DR STRING; 127582.A0A2Y9D6K0; -.
DR GeneID; 101357085; -.
DR KEGG; tmu:101357085; -.
DR InParanoid; A0A2Y9D6K0; -.
DR OrthoDB; 1110761at2759; -.
DR Proteomes; UP000248480; Unplaced.
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; IPR031688; CAC1F_C.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR005452; LVDCC_a1dsu.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR005446; VDCC_L_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:SF11; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1D; 1.
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; PR01636; LVDCCALPHA1D.
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};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|PIRSR:PIRSR602077-3};
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:UP000248480};
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 129..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 542..560
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 580..603
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 672..691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 744..771
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 906..924
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 944..964
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 976..1002
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1022..1052
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1149..1174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1228..1246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1258..1278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1368..1386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1460..1483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1617..1651
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1724..1823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1906..1940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..857
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1756..1785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1801..1823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 724
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 2179 AA; 247163 MW; B0857B7D9F0677DC CRC64;
MMMMMMMKKM QHQRQQADHA NEANYARGTR LPLSGEGPTS QPNSSKQTVL SWQAAIDAAR
QAKAAQTMST SAPPPVGSLS QRKRQQYAKS KKQGNSSNSR PARALFCLSL NNPIRRACIS
IVEWKPFDIF ILLAIFANCV ALAIYIPFPE DDSNSTNHNL EKVEYAFLII FTVETFLKII
AYGLLLHPNA YVRNGWNLLD FVIVIVGLFS VILEQLTKET EAGNHSSGKS GGFDVKALRA
FRVLRPLRLV SGVPSLQVVL NSIIKAMVPL LHIALLVLFV IIIYAIIGLE LFIGKMHKTC
FFADSDIVAE EDPAPCAFSG NGRQCTANDT ECRSGWVGPN GGITNFDNFA FAMLTVFQCI
TMEGWTDVLY WVNDAIGWEW PWVYFVSLII LGSFFVLNLV LGVLSGEFSK EREKAKARGD
FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEEEGGEEGK RNTSMPTSET ESVNTENVSG
EGENQGCCGS LWCWWKRRGA AKAGPSGCRR WGQAISKSKL SRRWRRWNRF NRRRCRAAVK
SVTFYWLVIV LVFLNTLTIS SEHYNQPDWL TQIQDIANKV LLALFTCEML VKMYSLGLQA
YFVSLFNRFD CFVVCGGITE TILVELEIMS PLGISVFRCV RLLRIFKVTR HWTSLSNLVA
SLLNSMKSIA SLLLLLFLFI IIFSLLGMQL FGGKFNFDET LTKRSTFDNF PQALLTVFQI
LTGEDWNAVM YDGIMAYGGP SSSGMIVCIY FIILFICGNY ILLNVFLAIA VDNLADAESL
NTAQKEEAEE KERKKIARKE SLENKKNNKP EVNQIANSDN KVTIDDYREE DEDKDPYPPC
DVPVGEEEEE EEEDEPEVPA GPRPRRISEL NMKEKIIPIP EGSAFFILSK TNPIRVGCHK
LINHHIFTNL ILVFIMLSSA ALAAEDPIRS HSFRNTILGY FDYAFTAIFT VEILLKMTTF
GAFLHKGAFC RNYFNLLDML VVGVSLVSFG IQSSAISVVK ILRVLRVLRP LRAINRAKGL
KHVVQCVFVA IRTIGNIMIV TTLLQFMFAC IGVQLFKGKF YRCTDEAKSN PEECRGLFIL
YKDGEVDNPV VRERIWQNSD FNFDNVLSAM MALFTVSTFE GWPALLYKAI DSNGENIGPI
YNYRVEISIF FIIYIIIVAF FMMNIFVGFV IVTFQEQGEK EYKNCELDKN QRQCVEYALK
ARPLRRYIPK NPYQYKFWYV VNSSPFEYMM FVLIMLNTLC LAMQHYEQSK MFNDAMDILN
MVFTGVFTVE MVLKVIAFKP KGYFSDAWNT FDSLIVIGSI IDVALSEADP TESENIPVPT
AAPGNSEESN RISITFFRLF RVMRLVKLLS RGEGIRTLLW TFIKSFQALP YVALLIAMLF
FIYAVIGMQM FGKVAMRDNN QINRNNNFQT FPQAVLLLFR CATGEAWQEI MLACLPGKLC
DPESDYNPGE EYTCGSNFAI VYFISFYMLC AFLIINLFVA VIMDNFDYLT RDWSILGPHH
LDEFKRIWSE YDPEAKGRIK HLDVVTLLRR IQPPLGFGKL CPHRVACKRL VAMNMPLNSD
GTVMFNATLF ALVRTALKIK TEGNLEQANE ELRAVIKKIW KKTSMKLLDQ VVPPAGDDEV
TVGKFYATFL IQDYFRKFKK RKEQGLVGKY PAKNTTVALQ AGLRTLHDIG PEIRRAISCD
LQDDEPEETK LEEEEDLFKR NGALLGNHVN HVNSDRRDSL QQTNTAHRPL HVQRPSIPPA
SDTEKPLFPP AGNSVCHNHH NRNSIGKPIP NSTNANLNNA NMSKAAHGKR PSIGNLEHVS
ENGHHSSHKH DREPQRKSSI KRTRYYETYV RSDSGDEQLP AICREDPEIY SYFRDPRCLG
EQEYFSGEEC YEDDSSPTGS WHNYGYYSRS PGSSWDFERP RGYHHPQGFL EDADSPTCHD
SRRSPRRRLL PPTPTPHRRS SFNFECLRRQ GSQEEVPLSP AFPHRTALPL HLMQQQIMAV
AGLDSSKAQY SPSHSTRSWA TPPATPPYQD WTPCYTPLIQ VERSESLDQV NGSLPSLHRS
SWYTDEPDIA YRTFTPASLT VPSSFRNKNS DKQRSADSLV EAVLISEGLG RYARDPKFVS
ATKHEIADAC DLTIDEMESA ASHLLNGNMS PRANGDVGPI SHQQDYELQD FGPGYSDEEP
DPGRYEEDLA DEMICITTL
//
