GenomeNet

Database: UniProt
Entry: HVCN1_HUMAN
LinkDB: HVCN1_HUMAN
Original site: HVCN1_HUMAN 
ID   HVCN1_HUMAN             Reviewed;         273 AA.
AC   Q96D96; A8MQ37; B4DEB3; F8WCH5; Q6UW11; Q96IS5;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-SEP-2017, entry version 128.
DE   RecName: Full=Voltage-gated hydrogen channel 1;
DE   AltName: Full=Hydrogen voltage-gated channel 1;
DE            Short=HV1;
DE   AltName: Full=Voltage sensor domain-only protein;
GN   Name=HVCN1; Synonyms=VSOP; ORFNames=UNQ578/PRO1140;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Eye, Lung, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME REGULATION,
RP   AND MUTAGENESIS OF HIS-140; HIS-193; ARG-205; ARG-208 AND ARG-211.
RX   PubMed=16554753; DOI=10.1038/nature04700;
RA   Ramsey I.S., Moran M.M., Chong J.A., Clapham D.E.;
RT   "A voltage-gated proton-selective channel lacking the pore domain.";
RL   Nature 440:1213-1216(2006).
RN   [7]
RP   PHOSPHORYLATION AT THR-29 AND SER-97, MUTAGENESIS OF THR-29 AND
RP   SER-97, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20037153; DOI=10.1074/jbc.C109.082727;
RA   Musset B., Capasso M., Cherny V.V., Morgan D., Bhamrah M., Dyer M.J.,
RA   DeCoursey T.E.;
RT   "Identification of Thr29 as a critical phosphorylation site that
RT   activates the human proton channel Hvcn1 in leukocytes.";
RL   J. Biol. Chem. 285:5117-5121(2010).
RN   [8]
RP   FUNCTION, MUTAGENESIS OF ASP-112; HIS-140 AND HIS-193, SUBCELLULAR
RP   LOCATION, AND ENZYME REGULATION.
RX   PubMed=22020278; DOI=10.1038/nature10557;
RA   Musset B., Smith S.M., Rajan S., Morgan D., Cherny V.V.,
RA   Decoursey T.E.;
RT   "Aspartate 112 is the selectivity filter of the human voltage-gated
RT   proton channel.";
RL   Nature 480:273-277(2011).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 221-273, SUBUNIT, SUBCELLULAR
RP   LOCATION, COILED COIL, AND DOMAIN.
RX   PubMed=20147290; DOI=10.1074/jbc.M109.040360;
RA   Li S.J., Zhao Q., Zhou Q., Unno H., Zhai Y., Sun F.;
RT   "The role and structure of the carboxyl-terminal domain of the human
RT   voltage-gated proton channel Hv1.";
RL   J. Biol. Chem. 285:12047-12054(2010).
CC   -!- FUNCTION: Mediates the voltage-dependent proton permeability of
CC       excitable membranes. Forms a proton-selective channel through
CC       which protons may pass in accordance with their electrochemical
CC       gradient. Proton efflux, accompanied by membrane depolarization,
CC       facilitates acute production of reactive oxygen species in
CC       phagocytosis. {ECO:0000269|PubMed:16554753,
CC       ECO:0000269|PubMed:20037153, ECO:0000269|PubMed:22020278}.
CC   -!- ENZYME REGULATION: The dimers display cooperative channel gating
CC       (By similarity). The channel activity is inhibited by zinc ions.
CC       {ECO:0000250, ECO:0000269|PubMed:16554753,
CC       ECO:0000269|PubMed:22020278}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20147290}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC       membrane; Multi-pass membrane protein. Note=Detected mainly at
CC       intracellular membranes upon overexpression in HeLa cells
CC       (PuMed:20147290), but not in other cell types.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q96D96-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96D96-2; Sequence=VSP_034395;
CC       Name=3;
CC         IsoId=Q96D96-3; Sequence=VSP_034396;
CC         Note=No experimental confirmation available.;
CC       Name=4;
CC         IsoId=Q96D96-4; Sequence=VSP_045052;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Enriched in immune tissues, such as lymph
CC       nodes, B-lymphocytes, monocytes and spleen.
CC       {ECO:0000269|PubMed:16554753}.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position. Unlike other voltage-gated ion channels it
CC       lacks the pore domain. {ECO:0000269|PubMed:20147290}.
CC   -!- DOMAIN: The C-terminal coiled coil region mediates
CC       homodimerization and cooperative channel gating. It is essential
CC       for normal subcellular localization.
CC       {ECO:0000269|PubMed:20147290}.
CC   -!- PTM: Phosphorylation may enhance channel gating.
CC       {ECO:0000269|PubMed:20037153}.
CC   -!- SIMILARITY: Belongs to the hydrogen channel family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ89413.1; Type=Frameshift; Positions=164, 175; Evidence={ECO:0000305};
DR   EMBL; AY359054; AAQ89413.1; ALT_FRAME; mRNA.
DR   EMBL; AK293543; BAG57024.1; -; mRNA.
DR   EMBL; AC144522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471054; EAW97935.1; -; Genomic_DNA.
DR   EMBL; CH471054; EAW97936.1; -; Genomic_DNA.
DR   EMBL; BC007277; AAH07277.1; -; mRNA.
DR   EMBL; BC009731; AAH09731.1; -; mRNA.
DR   EMBL; BC032672; AAH32672.1; -; mRNA.
DR   CCDS; CCDS31900.1; -. [Q96D96-1]
DR   CCDS; CCDS58278.1; -. [Q96D96-4]
DR   RefSeq; NP_001035196.1; NM_001040107.1. [Q96D96-1]
DR   RefSeq; NP_001243342.1; NM_001256413.1. [Q96D96-4]
DR   RefSeq; NP_115745.2; NM_032369.3. [Q96D96-1]
DR   RefSeq; XP_005254005.1; XM_005253948.2. [Q96D96-1]
DR   RefSeq; XP_011537147.1; XM_011538845.1. [Q96D96-1]
DR   RefSeq; XP_011537148.1; XM_011538846.2. [Q96D96-1]
DR   RefSeq; XP_011537149.1; XM_011538847.1. [Q96D96-1]
DR   RefSeq; XP_016875516.1; XM_017020027.1. [Q96D96-1]
DR   UniGene; Hs.211511; -.
DR   UniGene; Hs.334637; -.
DR   PDB; 3A2A; X-ray; 2.00 A; A/B/C/D=221-273.
DR   PDBsum; 3A2A; -.
DR   ProteinModelPortal; Q96D96; -.
DR   SMR; Q96D96; -.
DR   BioGrid; 124053; 9.
DR   DIP; DIP-46112N; -.
DR   MINT; MINT-4724965; -.
DR   STRING; 9606.ENSP00000242607; -.
DR   GuidetoPHARMACOLOGY; 746; -.
DR   TCDB; 1.A.51.1.2; the voltage-gated proton channel (vpc) family.
DR   iPTMnet; Q96D96; -.
DR   PhosphoSitePlus; Q96D96; -.
DR   BioMuta; HVCN1; -.
DR   DMDM; 74751810; -.
DR   EPD; Q96D96; -.
DR   MaxQB; Q96D96; -.
DR   PaxDb; Q96D96; -.
DR   PeptideAtlas; Q96D96; -.
DR   PRIDE; Q96D96; -.
DR   DNASU; 84329; -.
DR   Ensembl; ENST00000242607; ENSP00000242607; ENSG00000122986. [Q96D96-1]
DR   Ensembl; ENST00000356742; ENSP00000349181; ENSG00000122986. [Q96D96-1]
DR   Ensembl; ENST00000439744; ENSP00000412052; ENSG00000122986. [Q96D96-4]
DR   Ensembl; ENST00000548312; ENSP00000449601; ENSG00000122986. [Q96D96-3]
DR   Ensembl; ENST00000620084; ENSP00000479812; ENSG00000122986. [Q96D96-1]
DR   GeneID; 84329; -.
DR   KEGG; hsa:84329; -.
DR   UCSC; uc001trq.1; human. [Q96D96-1]
DR   CTD; 84329; -.
DR   DisGeNET; 84329; -.
DR   EuPathDB; HostDB:ENSG00000122986.13; -.
DR   GeneCards; HVCN1; -.
DR   H-InvDB; HIX0011039; -.
DR   HGNC; HGNC:28240; HVCN1.
DR   HPA; HPA039329; -.
DR   MIM; 611227; gene.
DR   neXtProt; NX_Q96D96; -.
DR   OpenTargets; ENSG00000122986; -.
DR   PharmGKB; PA144596422; -.
DR   eggNOG; ENOG410IKBG; Eukaryota.
DR   eggNOG; ENOG4111XHU; LUCA.
DR   GeneTree; ENSGT00530000063670; -.
DR   HOGENOM; HOG000067871; -.
DR   HOVERGEN; HBG102207; -.
DR   InParanoid; Q96D96; -.
DR   OMA; RMSKFLK; -.
DR   OrthoDB; EOG091G0L8G; -.
DR   PhylomeDB; Q96D96; -.
DR   TreeFam; TF332056; -.
DR   Reactome; R-HSA-1300642; Sperm Motility And Taxes.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   ChiTaRS; HVCN1; human.
DR   GeneWiki; HVCN1; -.
DR   GenomeRNAi; 84329; -.
DR   PRO; PR:Q96D96; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000122986; -.
DR   CleanEx; HS_HVCN1; -.
DR   ExpressionAtlas; Q96D96; baseline and differential.
DR   Genevisible; Q96D96; HS.
DR   GO; GO:0016021; C:integral component of membrane; IDA:HGNC.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR   GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR   GO; GO:0022843; F:voltage-gated cation channel activity; TAS:Reactome.
DR   GO; GO:0030171; F:voltage-gated proton channel activity; IDA:UniProtKB.
DR   GO; GO:0071467; P:cellular response to pH; IDA:UniProtKB.
DR   GO; GO:0071294; P:cellular response to zinc ion; IDA:UniProtKB.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0015992; P:proton transport; IDA:UniProtKB.
DR   GO; GO:0009268; P:response to pH; ISS:HGNC.
DR   GO; GO:0010043; P:response to zinc ion; IDA:HGNC.
DR   GO; GO:0035036; P:sperm-egg recognition; TAS:Reactome.
DR   InterPro; IPR031846; Hvcn1.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR031844; VGPC1_C.
DR   PANTHER; PTHR12305:SF63; PTHR12305:SF63; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF16799; VGPC1_C; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Coiled coil;
KW   Complete proteome; Ion channel; Ion transport; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    273       Voltage-gated hydrogen channel 1.
FT                                /FTId=PRO_0000342187.
FT   TOPO_DOM      1    100       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    101    121       Helical; Name=Segment S1. {ECO:0000250}.
FT   TOPO_DOM    122    138       Extracellular. {ECO:0000250}.
FT   TRANSMEM    139    161       Helical; Name=Segment S2. {ECO:0000250}.
FT   TOPO_DOM    162    169       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    170    190       Helical; Name=Segment S3. {ECO:0000250}.
FT   TOPO_DOM    191    197       Extracellular. {ECO:0000250}.
FT   TRANSMEM    198    218       Helical; Name=Segment S4. {ECO:0000250}.
FT   TOPO_DOM    219    273       Cytoplasmic. {ECO:0000250}.
FT   COILED      223    266       {ECO:0000269|PubMed:20147290}.
FT   COMPBIAS     46     55       Poly-Glu.
FT   COMPBIAS    176    180       Poly-Val.
FT   MOD_RES      29     29       Phosphothreonine.
FT                                {ECO:0000305|PubMed:20037153}.
FT   MOD_RES      97     97       Phosphoserine.
FT                                {ECO:0000305|PubMed:20037153}.
FT   VAR_SEQ       1     20       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_045052.
FT   VAR_SEQ      66    102       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_034395.
FT   VAR_SEQ     253    273       EQEIERLNKLLRQHGLLGEVN -> PLD (in isoform
FT                                3). {ECO:0000303|PubMed:12975309}.
FT                                /FTId=VSP_034396.
FT   MUTAGEN      29     29       T->A: Loss of a phosphorylation site.
FT                                Reduces phosphorylation.
FT                                {ECO:0000269|PubMed:20037153}.
FT   MUTAGEN      97     97       S->A: Loss of a phosphorylation site.
FT                                Strongly reduces phosphorylation.
FT                                {ECO:0000269|PubMed:20037153}.
FT   MUTAGEN     112    112       D->A,F,N,S: Alters channel selectivity.
FT                                Converts the proton channel to an anion
FT                                channel. {ECO:0000269|PubMed:22020278}.
FT   MUTAGEN     112    112       D->E: No effect on channel activity and
FT                                proton selectivity.
FT                                {ECO:0000269|PubMed:22020278}.
FT   MUTAGEN     112    112       D->V: Abolishes channel activity.
FT                                {ECO:0000269|PubMed:22020278}.
FT   MUTAGEN     140    140       H->A: Exhibits selectivity to protons but
FT                                sensitivity to zinc ions is abolished;
FT                                when associated with A-193.
FT                                {ECO:0000269|PubMed:16554753,
FT                                ECO:0000269|PubMed:22020278}.
FT   MUTAGEN     193    193       H->A: Exhibits selectivity to protons but
FT                                sensitivity to zinc ions is abolished;
FT                                when associated with A-140.
FT                                {ECO:0000269|PubMed:16554753,
FT                                ECO:0000269|PubMed:22020278}.
FT   MUTAGEN     205    205       R->A: Faster channel activation and
FT                                deactivation kinetics.
FT                                {ECO:0000269|PubMed:16554753}.
FT   MUTAGEN     208    208       R->A: Faster channel activation and
FT                                deactivation kinetics.
FT                                {ECO:0000269|PubMed:16554753}.
FT   MUTAGEN     211    211       R->A: Faster channel deactivation
FT                                kinetics. {ECO:0000269|PubMed:16554753}.
FT   CONFLICT    165    165       F -> Y (in Ref. 2; BAG57024).
FT                                {ECO:0000305}.
FT   HELIX       227    265       {ECO:0000244|PDB:3A2A}.
SQ   SEQUENCE   273 AA;  31683 MW;  0F93B428AECBBC4F CRC64;
     MATWDEKAVT RRAKVAPAER MSKFLRHFTV VGDDYHAWNI NYKKWENEEE EEEEEQPPPT
     PVSGEEGRAA APDVAPAPGP APRAPLDFRG MLRKLFSSHR FQVIIICLVV LDALLVLAEL
     ILDLKIIQPD KNNYAAMVFH YMSITILVFF MMEIIFKLFV FRLEFFHHKF EILDAVVVVV
     SFILDIVLLF QEHQFEALGL LILLRLWRVA RIINGIIISV KTRSERQLLR LKQMNVQLAA
     KIQHLEFSCS EKEQEIERLN KLLRQHGLLG EVN
//
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