ID A0A2K6U3Q4_SAIBB Unreviewed; 2171 AA.
AC A0A2K6U3Q4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1D {ECO:0000313|Ensembl:ENSSBOP00000026504.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000026504.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000026504.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSSBOT00000043377.1; ENSSBOP00000026504.1; ENSSBOG00000029562.1.
DR GeneTree; ENSGT00940000154839; -.
DR Proteomes; UP000233220; 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; 3.
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:UP000233220};
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 154..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 547..565
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 585..608
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 677..696
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 749..776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 911..929
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 949..969
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 981..1007
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1027..1057
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1154..1179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1263..1283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1358..1376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1450..1473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1607..1641
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 88..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1668..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1694..1813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2118..2162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..846
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..862
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1706..1721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1791..1810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 729
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 2171 AA; 246451 MW; 64BADB4234DB5F62 CRC64;
MEMNLPTFSS DLILIKNALY QEIDARYKGK VISEAEMKGY FSLAFEEANY ARGTRLPLSG
EGPTSQPNSS KQTVLSWQAA IDAARQAKAA QTMSTSAPPP VGSLSQRKRQ QYAKSKKQGN
SSNSRPARAL FCLSLNNPIR RACISIVEWK PFDIFILLAI FANCVALAIY IPFPEDDSNS
TNHNLEKVEY AFLIIFTVET FLKIIAYGLL LHPNAYVRNG WNLLDFVIVI VGLFSVILEQ
LTKETEGGNH SSGKSGGFDV KALRAFRVLR PLRLVSGVPS LQVVLNSIIK AMVPLLHIAL
LVLFVIIIYA IIGLELFIGK MHKTCFFADS DIVAEEDPAP CAFSGNGRQC TANGTECRSG
WVGPNGGITN FDNFAFAMLT VFQCITMEGW TDVLYWVNDA IGWEWPWVYF VSLIILGSFF
VLNLVLGVLS GEFSKEREKA KARGDFQKLR EKQQLEEDLK GYLDWITQAE DIDPENEEEG
GEEGKRNTSM PTSETESVNT ENVSGEAETR GCCGSLCQAI SKSKLSRRWR RWNRFNRRRC
RAAVKSVTFY WLVIVLVFLN TLTISSEHYN QPDWLTQIQD IANKVLLALF TCEMLVKMYS
LGLQAYFVSL FNRFDCFVVC GGITETILVE LEIMSPLGIS VFRCVRLLRI FKVTRHWTSL
SNLVASLLNS MKSIASLLLL LFLFIIIFSL LGMQLFGGKF NFDETQTKRS TFDNFPQALL
TVFQILTGED WNAVMYDGIM AYGGPSSSGM IVCIYFIILF ICGNYILLNV FLAIAVDNLA
DAESLNTAQK EEAEEKERKK IARKESLENK KNNKPEVNQI ANSDNKVTID DYREEDEDKD
PYPPCDVPVG EEEEEEEEDE PEVPAGPRPR RISELNMKEK IAPIPEGSAF FILSKTNPIR
VGCHKLINHH IFTNLILVFI MLSSAALAAE DPIRSHSFRN TILGYFDYAF TAIFTVEILL
KMTTFGAFLH KGAFCRNYFN LLDMLVVGVS LVSFGIQSSA ISVVKILRVL RVLRPLRAIN
RAKGLKHVVQ CVFVAIRTIG NIMIVTTLLQ FMFACIGVQL FKGKFYRCTD EAKSNPEECR
GLFILYKDGD VDSPVVRERI WQNSDFNFDN VLSAMMALFT VSTFEGWPAL LYKAIDSNGE
NVGPVYNHRV EISIFFIIYI IIVAFFMMNI FVGFVIVTFQ EQGEKEYKNC ELDKNQRQCV
EYALKARPLR RYIPKNPYQY TFWYVVNSSP FEYMMFVLIM LNTLCLAMQH YEQSKMFNDA
MDILNMVFTG VFTVEMVLKV IAFKPKGYFS DAWNTFDSLI VIGSIIDVAL SEADNSEESN
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 PAKNTTIALQ AGLRTLHDIG PEIRRAISCD LQDDEPEETK
REEDDDVFKR NGALLGNHVN HVNSDRRDSL QQTNTTHRPL HVQRPSIPPA SDTEKPLFPP
AGNSVCHNHH NHNSIGKQAP TSTNANLNNA NMSKAAHGKR PSLGNLEHVS ENGHHSSHKH
DREPQRRSSV QRTRYYETYI RSDSGDEQLP TICREDPEIC GYFRDPRCLG EQEYFSSEEC
YEDDSSPTWS RQNYGYYRRY PSRNVDFERP RGYHQPQGFL EDDDSPICYD SRRSPRRRLL
PPTPASHRRS SFNFECLRRQ SSQEEIPSSP TFFPHRTALP LHLMQQQIMA VAGLDSSKAQ
KYSPSHSTRS WATPPATPPY RDWTPCYTPL IQVEQSEALD QVNGSLPSLH RSSWYTDEPD
ISYRTFTPAS LTIPSSFRNK NSDKQRSADS LVEAVLISEG LGRYARDPKF VSATKHEIAD
ACDLTIDEME SAASTLLNGN MRPRANGDVG PLSHQQDYEL QDFGPGYSDE EPDPGRDEED
LADEMICITT L
//
