ID A0A093Q8N8_9PASS Unreviewed; 2111 AA.
AC A0A093Q8N8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Voltage-dependent N-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
DE Flags: Fragment;
GN ORFNames=N305_07766 {ECO:0000313|EMBL:KFW82785.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW82785.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW82785.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW82785.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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. This alpha-1B subunit gives rise to N-type
CC calcium currents. N-type calcium channels belong to the 'high-voltage
CC activated' (HVA) group. They are involved in pain signaling. Calcium
CC channels containing alpha-1B subunit may play a role in directed
CC migration of immature neurons. {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. CACNA1B subfamily. {ECO:0000256|ARBA:ARBA00005685}.
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DR EMBL; KL671500; KFW82785.1; -; Genomic_DNA.
DR STRING; 328815.ENSMVIP00005011658; -.
DR Proteomes; UP000053258; Unassembled WGS sequence.
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; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR005447; VDCC_N_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:SF6; VOLTAGE-DEPENDENT N-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1B; 1.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01631; NVDCCALPHA1.
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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000053258};
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 133..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 495..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 594..616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 672..694
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1043..1062
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1082..1103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1115..1133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1176..1198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1288..1313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1369..1387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1399..1422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1491..1518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1578..1602
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1738..1772
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1869..1925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1942..2111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 703..730
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 834..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1946..1964
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1984..2005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2013..2027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2028..2104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 310
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT NON_TER 2111
FT /evidence="ECO:0000313|EMBL:KFW82785.1"
SQ SEQUENCE 2111 AA; 239446 MW; A2B2C62AE1B28912 CRC64;
MARFGDDRPP RYGGGGPAGA GRGSSRQGGP QAGQRMYKQS MAQRARTMAL YNPIPVKQNC
FTVNRSLFIF SEDNVIRKYA KRITEWPYPF RKAVWVRGEA TIIANCIVLA LEQHLPDGDK
TPMSERLDDT EPYFIGIFCF EAGIKIIALG FVFHKGSYLR NGWNVMDFVV VLTGILATAG
TDFDLRTLRA VRVLRPLKLV SGIPSLQVVL KSIMKAMVPL LQIGLLLFFA IVMFAIIGLE
FYMGKFHKTC FSNETGDEVG DFPCGEEPPA RQCESGTTCR EYWQGPNYGI TNFDNILFAV
LTVFQCITME GWTDILYNTN DAAGNTWNWL YFIPLIIIGS FFMLNLVLGV LSGEFAKERE
RVENRRAFLK LRRQQQIERE LNGYLEWIFK AEEVMLAEED KNAEEKSPLD VLKRAAIKKS
KNDLIHAEEG SPFARASLKS GKNESSSYFR RKEKMFRFFI RRMVKAQSFY WIVLCVVALN
TLCVAMVHYD QPEKLTTALY FAEFVFLGLF LTEMSLKMYG LGPRNYFHSS FNCFDFGVIV
GSIFEVIWAA VKPGTSFGIS VLRALRLLRI FKVTKYWNSL RNLVVSLLNS MKSIISLLFL
LFLFIVVFAL LGMQLFGGQF NFQDETPTTN FDTFPAAILT VFQILTGEDW NAVMYHGIES
QGGVRSGMFS SIYFIVLTLF GNYTLLNVFL AIAVDNLANA QELTKDEEEM EEATNQKLAL
QKAKEVAEVS PMSAANISIA AKQQNSSKSK SVWEQRTSQI RMHNFRASCE ALYNELDPEE
RVRYATTLHI RPDMKTHLDR PLVVEPRSEG RNNINKLSPG DVQEVQEHPK GGSADGAEAP
RKHHRHRDKE KQAEQEKGDA PKGSRSGNRD GEPKGENGEE PHRRHRLRNR ALSTYESVEK
ENGEKEAEAG EKEHRNHQPK ENQVELEASG SVSVPVHTLP STYLQKVPEQ PEDADNQKNV
TRMIQPPLDK TTTVNIPVTI TAPPGETTVI PMNNVEFESK TEEKKDVDDL TKNGPKAILP
YSSMFILSPT NPIRRLFHYI VNLRYFEMVI LIVIALSSIA LAAEDPVQAE SPRNDALKYL
DYIFTGVFTF EMVIKMIDLG LLLHPGSYFR DLWNILDFIV VSGALVAFAF SGTKGKDINT
IKSLRVLRVL RPLKTIKRLP KLKAVFDCVV NSLKNVLNIL IVYMLFMFIF AVIAVQLFKG
RFFYCTDESK ELEKDCRGQY LDYEKNEVEA QPREWKKYEF HYDNVLWALL TLFTVSTGEG
WPTVLKHSVD ATYEEQGPSP GYRMEMSIFY VVYFVVFPFF FVNIFVALII ITFQEQGDKV
MSECSLEKNE RACIDFAISA KPLTRYMPQN KQSFQYKMWK FVVSPPFEYF IMVMIALNTI
VLMMKFYDAP EAYEEMLKCL NIVFTSMFSM ECVLKIIAFG VLNYFRDAWN VFDFVTVLGS
ITDILVTEIA DNFINLSFLR LFRAARLIKL LRQGYTIRIL LWTFVQSFKA LPYVCLLIAM
LFFIYAIIGM QVFGNIALDD ETSINRHNNF RTFLQALMLL FRSATGEAWH EIMLSCLSNR
ACDPLSGLTK KECGSDFAYF YFVSFIFLCS FLMLNLFVAV IMDNFEYLTR DSSILGPHHL
DEFVRVWAEY DPAACCRIHY KDMYNLLRVI APPLGLGKKC PHRVAYKRLV RMNMPISPED
LTVHFTSTLM ALIRTALEIK LASGGVKQHQ CDAELRKEIS LVWPNLSQKT LDLLVPPPDE
MTVGKVYAAL MIFDFYKQNK NSREQVQPPG GLCQPGPVSL FHPLKATLEQ TQPTAFNNAK
AFLRQKSSAS LNNGGALPAP EGGIKESSSW GTQRTQDVFY ETRTPAFERG HSEEIPIERV
VEMREISPTV ANGEPQPGLE SQGRAASMPR LAAETKRSKA RSPGSYLAPI PDTSPMKRSV
STLTPQRPHA MHLYEYSLER MPPEQGHHHH HHRCHRRKEK KQKSLDRAAH HLADGQAAAQ
AGESSGKDKK ERGRSQERKQ HSSSSSEKQR FYSCDRYGSR ERSQTKSAEQ SRPTSPNGGP
EQGPHRQGSG SVNGSPLLST SGASTPCRGR RQLPQTPLTP RPSITYKTAN SSPVHFTSIQ
PGLPTFSPGR L
//
