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Database: UniProt
Entry: TPC2_DANRE
LinkDB: TPC2_DANRE
Original site: TPC2_DANRE 
ID   TPC2_DANRE              Reviewed;         774 AA.
AC   A0JMD4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   27-SEP-2017, entry version 64.
DE   RecName: Full=Two pore calcium channel protein 2;
DE   AltName: Full=Voltage-dependent calcium channel protein TPC2;
GN   Name=tpcn2; Synonyms=tpc2; ORFNames=zgc:152898;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Nicotinic acid adenine dinucleotide phosphate (NAADP)
CC       receptor that may function as one of the major voltage-gated
CC       Ca(2+) channels (VDCC) across the lysosomal membrane. May be
CC       involved in smooth muscle contraction (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Note=Only the acidic lysosomal
CC       fraction is sensitive to NAADP. {ECO:0000250}.
CC   -!- DOMAIN: Each of the two internal repeats contains five hydrophobic
CC       transmembrane segments (S1, S2, S3, S5, S6) and one positively
CC       charged transmembrane segment (S4). S4 segments probably represent
CC       the voltage-sensor and are characterized by a series of positively
CC       charged amino acids at every third position (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. Two pore calcium channel subfamily.
CC       {ECO:0000305}.
DR   EMBL; BC125833; AAI25834.1; -; mRNA.
DR   RefSeq; NP_001071190.1; NM_001077722.1.
DR   UniGene; Dr.133033; -.
DR   UniGene; Dr.156799; -.
DR   ProteinModelPortal; A0JMD4; -.
DR   STRING; 7955.ENSDARP00000077125; -.
DR   PaxDb; A0JMD4; -.
DR   GeneID; 777614; -.
DR   KEGG; dre:777614; -.
DR   CTD; 219931; -.
DR   ZFIN; ZDB-GENE-061103-202; tpcn2.
DR   eggNOG; ENOG410INF2; Eukaryota.
DR   eggNOG; ENOG410XNV2; LUCA.
DR   HOGENOM; HOG000154668; -.
DR   HOVERGEN; HBG079776; -.
DR   InParanoid; A0JMD4; -.
DR   KO; K14077; -.
DR   PhylomeDB; A0JMD4; -.
DR   PRO; PR:A0JMD4; -.
DR   Proteomes; UP000000437; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0072345; F:NAADP-sensitive calcium-release channel activity; ISS:UniProtKB.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   GO; GO:0006939; P:smooth muscle contraction; ISS:UniProtKB.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR028798; TPC2.
DR   PANTHER; PTHR10037:SF270; PTHR10037:SF270; 1.
DR   Pfam; PF00520; Ion_trans; 2.
PE   2: Evidence at transcript level;
KW   Calcium; Calcium channel; Calcium transport; Complete proteome;
KW   Glycoprotein; Ion channel; Ion transport; Lysosome; Membrane;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   CHAIN         1    774       Two pore calcium channel protein 2.
FT                                /FTId=PRO_0000276858.
FT   TOPO_DOM      1     92       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     93    113       Helical; Name=S1 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    114    140       Extracellular. {ECO:0000255}.
FT   TRANSMEM    141    161       Helical; Name=S2 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    162    170       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    171    191       Helical; Name=S3 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    192    197       Extracellular. {ECO:0000255}.
FT   TRANSMEM    198    218       Helical; Name=S4 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    219    232       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    233    253       Helical; Name=S5 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    254    267       Extracellular. {ECO:0000255}.
FT   INTRAMEM    268    292       Helical; Pore-forming. {ECO:0000255}.
FT   TOPO_DOM    293    302       Extracellular. {ECO:0000255}.
FT   TRANSMEM    303    323       Helical; Name=S6 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    324    452       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    453    475       Helical; Name=S1 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    476    486       Extracellular. {ECO:0000255}.
FT   TRANSMEM    487    507       Helical; Name=S2 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    508    518       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    519    539       Helical; Name=S3 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    540    564       Extracellular. {ECO:0000255}.
FT   TRANSMEM    565    585       Helical; Name=S4 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    586    596       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    597    617       Helical; Name=S5 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    618    658       Extracellular. {ECO:0000255}.
FT   INTRAMEM    659    681       Helical; Pore-forming. {ECO:0000255}.
FT   TOPO_DOM    682    696       Extracellular. {ECO:0000255}.
FT   TRANSMEM    697    717       Helical; Name=S6 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    718    774       Cytoplasmic. {ECO:0000255}.
FT   CARBOHYD    626    626       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    632    632       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    637    637       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   774 AA;  89184 MW;  25C167D2C54FEA9E CRC64;
     MEEEPLLAGS INQGSGDYGA HSESCLHYPD EHTPRSRRLS YSVTDDSCNV EEDADADLYV
     QQAVVFIEDA IKYRSINHRV DSGSLRLYRW YYSNLCQWGL GLTIAVVLAL AFIERPSSLT
     YTSDIRVKPK PWEPPCGMTE GIEIVCLCIF ILDVTAKGYL IGWEEFRMNK WLLAYLIVIT
     ASVIDWMLSI SMLCDENLRV RRLIRPFFLL QNSSLMKKTL KCIKRTLPEI ASVILLLALH
     ICLFTMIGML IFAKSDDPKQ NGEWQTYFRN LPKALSSLLV LLTTANNPDV MIPAYSLNRG
     YSIFFILFSV FGTYLLMNLM TAIIYNQFRG YLLMSVQTSI IRRRLGIRAA FEVLCCPGRG
     HTSTQAEGHV ERVAVSMFLK VMERVHMKSY CRQAIVKAAR RFPDGFISGE DFQRLFNELD
     KDFVKEHPPK PEYSSSGLQH IQYVYSHYYI SVLGNAVALA NVICICTVLV LNAEKSASEK
     NYFYMEIINC IFILYYLIEM LLKIVAFGWK GYLSYRNNIF DGFLTVLLLA IQIVIFITFK
     IPYVDVDPVP RHVMALWEMI RLVNMLIVFR FLRIIPEIKL MAVVASTIVD LVKNLRAFAG
     ILLVVYYMFA VLGIWLFQGA ISPPSNMSLV SNSSLENITG PYSMECGTFE QLEYWPNNFD
     DFASSLILLY NIMVVNNWHV FTDAYARYTT DWSLVYFVVW WLTSSVMWVN LFVALILENF
     TYKWDRSNGL SVEDVERIAY QSTVQLMFKE HVKEPTEEEL LAQLHQHPHL HLSW
//
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