ID A0A2G8KU77_STIJA Unreviewed; 1209 AA.
AC A0A2G8KU77;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative voltage-dependent P/Q-type calcium channel subunit alpha-1A-like {ECO:0000313|EMBL:PIK51557.1};
GN ORFNames=BSL78_11548 {ECO:0000313|EMBL:PIK51557.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK51557.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK51557.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK51557.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK51557.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIK51557.1}.
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DR EMBL; MRZV01000366; PIK51557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8KU77; -.
DR STRING; 307972.A0A2G8KU77; -.
DR Proteomes; UP000230750; 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 Gene3D; 1.10.287.70; -; 3.
DR Gene3D; 6.10.250.2180; -; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 3.
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; 3.
DR PRINTS; PR00167; CACHANNEL.
DR SMART; SM01062; Ca_chan_IQ; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 3.
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};
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:UP000230750};
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 37..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 411..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 441..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..513
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 556..574
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..627
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 683..703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 715..735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 747..766
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 806..829
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 850..872
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 892..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 931..966
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 289..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1156
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 575
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 1209 AA; 139377 MW; CF52E1ECCB1F094B CRC64;
MRYTEKKKSE KKYCVSFRST EKRFRFTVRR LVKSQPMYWA VIVLVFLNTL CVSIEHYGQP
DYLDEFLRVA EITFLCIFII EMLVKMYGLG PRVYLQSSFN KFDCLVILAS LFEVIWSNYN
KASFGLSVLR ALRLLRIFKV TRYWSSLRNL VISLLSSMRS IVSLLFLLFL FILIFALLGM
QLFGGSFNFN HREAKPTSNF DTFPIALMTV FQILTGEDWN TVMYYGIESQ GGVEKGMFAS
IYFVILVLFG NYTLLNVFLA IAVDNLANAQ ELTRLDKVDE EEAREQIERE VEALTNTPRT
SRRTSPLAIE DGQSKDTKGQ GLNGDHQEPE PGTEEEDDEN IFTPKPMVPY SSLFIFSTTN
PLRTFCHYIV NLRYFDLMIM IVIGMSSIAL AAEDPLDSTN VRNGILKKFD YAFTGIFTIE
LILKIIDMGL FLHKGSYCRD LWNILDAVVV VCALVAFVVE SGNSNGQLGT IKSLRVLRAV
FDCVLNSVKN VTNIAIVYLL FMFIFAVIGV QLYKGKFYYC TDGAKIYEHE CQGSYFEFDG
DQISEQKKRE WELYDFNFNN IFMALLTLFT VSTGEGWPDV LKHSIDSTDE GRGPEPYNSI
QNALYYVVYF IIFPFFFLNI FVALIIITFQ EQGDQEYDDG DIDKNQKQCI EFCINATPVN
MFVPSDKNSF KYKFWKFVVS PPFEYFIMTL IALNTIILML KHYNATEEFE DVMKTLNIIF
TVLFSIEAVL KLIAFGPRNY FRDGWNVFDF ITVVGSILDV IITELSDTFV NLTVLRLFRA
ARLIKLLRQG SSIRILLWTF LQSIKALPWV CLLIGMLFFI YAIIGMQVFG GIKQNEPGSI
ITSYSNFSNF FWSLLLLFRC ATGESWQLIM LACLDGTCHE NPEENCGSPF SYPYFVSFIF
LCSFLMLNLF VAVIMDNFDY LTRDASILGA HHLDEYVRVW GDYDPAGTGR INYKEMYEML
KEMEPPVGFG RNCPYRIAYK RLIRMNMPVA EDKTVGFRTT LMALIRTALD IKIGNVADRD
RHDTELREAI VTFWPTMSDD KLDLLVPPDS ELVGEKLTVG KIYAALLIYE TWREYKAKVQ
RDGHARTQRY QLRLAYIEQI KAREQEMLML EEEKQRREYY GEEEDEDGEY VDGADEALYD
DDEQDSGDDD DDIYEDAIPT VVMTNPHEEP VKNHTRENEV YENDANGTPK GKSRNGTGRK
PRQRCTGTT
//
