MCLN2_HUMAN
ID MCLN2_HUMAN Reviewed; 566 AA.
AC Q8IZK6; A6NI99; Q2M3I6; Q5TAG5; Q8N9R3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Mucolipin-2;
DE AltName: Full=Transient receptor potential channel mucolipin 2;
DE Short=TRPML2;
GN Name=MCOLN2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=12403827; DOI=10.1073/pnas.222425399;
RA Di Palma F., Belyantseva I.A., Kim H.J., Vogt T.F., Kachar B.,
RA Noben-Trauth K.;
RT "Mutations in Mcoln3 associated with deafness and pigmentation defects in
RT varitint-waddler (Va) mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14994-14999(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-249 (ISOFORM 1).
RC TISSUE=Uterus;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 463-ASP-ASP-464.
RX PubMed=17662026; DOI=10.1111/j.1600-0854.2007.00619.x;
RA Karacsonyi C., Miguel A.S., Puertollano R.;
RT "Mucolipin-2 localizes to the Arf6-associated pathway and regulates
RT recycling of GPI-APs.";
RL Traffic 8:1404-1414(2007).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF 463-ASP-ASP-464.
RX PubMed=19940139; DOI=10.1074/jbc.m109.046508;
RA Lev S., Zeevi D.A., Frumkin A., Offen-Glasner V., Bach G., Minke B.;
RT "Constitutive activity of the human TRPML2 channel induces cell
RT degeneration.";
RL J. Biol. Chem. 285:2771-2782(2010).
RN [8]
RP SUBUNIT, AND FUNCTION.
RX PubMed=19885840; DOI=10.1002/jcp.21956;
RA Curcio-Morelli C., Zhang P., Venugopal B., Charles F.A., Browning M.F.,
RA Cantiello H.F., Slaugenhaupt S.A.;
RT "Functional multimerization of mucolipin channel proteins.";
RL J. Cell. Physiol. 222:328-335(2010).
RN [9]
RP INTERACTION WITH TMEM176A.
RX PubMed=25130899; DOI=10.1111/tra.12205;
RA Cuajungco M.P., Basilio L.C., Silva J., Hart T., Tringali J., Chen C.C.,
RA Biel M., Grimm C.;
RT "Cellular zinc levels are modulated by TRPML1-TMEM163 interaction.";
RL Traffic 15:1247-1265(2014).
CC -!- FUNCTION: Nonselective cation channel probably playing a role in the
CC regulation of membrane trafficking events. Acts as Ca(2+)-permeable
CC cation channel with inwardly rectifying activity (PubMed:19940139,
CC PubMed:19885840). May activate ARF6 and be involved in the trafficking
CC of GPI-anchored cargo proteins to the cell surface via the ARF6-
CC regulated recycling pathway (PubMed:17662026). May play a role in
CC immune processes. In adaptive immunity, TRPML2 and TRPML1 may play
CC redundant roles in the function of the specialized lysosomes of B cells
CC (By similarity). In the innate immune response, may play a role in the
CC regulation of chemokine secretion and macrophage migration (By
CC similarity). Through a possible and probably tissue-specific
CC heteromerization with MCOLN1 may be at least in part involved in many
CC lysosome-dependent cellular events (PubMed:19885840).
CC {ECO:0000250|UniProtKB:Q8K595, ECO:0000269|PubMed:17662026,
CC ECO:0000269|PubMed:19885840, ECO:0000269|PubMed:19940139, ECO:0000305}.
CC -!- ACTIVITY REGULATION: Channel activity is reduced by low
CC extracellular/lumenal pH level (PubMed:19940139).
CC {ECO:0000269|PubMed:19940139, ECO:0000305}.
CC -!- SUBUNIT: Forms homooligomeric complexes; probably tetrameric (By
CC similarity). Can heterooligomerize with MCOLN1; heteromeric assemblies
CC have different channel properties as compared to the respective
CC homooligomers and may be tissue-specific (PubMed:19885840). Interacts
CC with TMEM176A (PubMed:25130899). {ECO:0000250|UniProtKB:Q9GZU1,
CC ECO:0000269|PubMed:19885840, ECO:0000269|PubMed:25130899}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17662026};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Late
CC endosome membrane {ECO:0000269|PubMed:17662026}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:F6RG56}. Lysosome membrane
CC {ECO:0000269|PubMed:17662026}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:F6RG56}. Recycling endosome membrane
CC {ECO:0000269|PubMed:17662026}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:F6RG56}. Note=Localizes to recycling endosomes
CC in activated macrophages and microglia. {ECO:0000250|UniProtKB:Q8K595}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IZK6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZK6-2; Sequence=VSP_034642;
CC -!- DOMAIN: The most N-terminal extracellular/lumenal domain (referred to
CC as I-II linker or polycystin-mucolipin domain) contributes to a
CC structure with a four-fold rotational symmetry in a tetrameric
CC assembly; the structure contains a central highly electronegative pore
CC with a 14 A diameter. The pore is critical for Ca(2+) and pH
CC regulation. The protruding structure formed by the I-II linkers may
CC contain all the interaction sites with lipids and proteins in the
CC endolysosomal lumen. {ECO:0000250|UniProtKB:Q9GZU1}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
CC Polycystin subfamily. MCOLN2 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC04267.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY083533; AAM08926.1; -; mRNA.
DR EMBL; AL139150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW73221.1; -; Genomic_DNA.
DR EMBL; BC104891; AAI04892.1; -; mRNA.
DR EMBL; BC104893; AAI04894.1; -; mRNA.
DR EMBL; AK094010; BAC04267.1; ALT_SEQ; mRNA.
DR CCDS; CCDS30762.1; -. [Q8IZK6-1]
DR CCDS; CCDS81347.1; -. [Q8IZK6-2]
DR RefSeq; NP_001317576.1; NM_001330647.1. [Q8IZK6-2]
DR RefSeq; NP_694991.2; NM_153259.3. [Q8IZK6-1]
DR RefSeq; XP_005270776.1; XM_005270719.3. [Q8IZK6-2]
DR RefSeq; XP_011539489.1; XM_011541187.2. [Q8IZK6-2]
DR RefSeq; XP_011539490.1; XM_011541188.2. [Q8IZK6-2]
DR PDB; 6HRR; X-ray; 2.00 A; A/B=92-282.
DR PDB; 6HRS; X-ray; 2.95 A; A/B/C/D/E/F/G/H=86-284.
DR PDBsum; 6HRR; -.
DR PDBsum; 6HRS; -.
DR AlphaFoldDB; Q8IZK6; -.
DR SASBDB; Q8IZK6; -.
DR SMR; Q8IZK6; -.
DR BioGRID; 129087; 32.
DR IntAct; Q8IZK6; 1.
DR STRING; 9606.ENSP00000359640; -.
DR GuidetoPHARMACOLOGY; 502; -.
DR TCDB; 1.A.5.3.3; the polycystin cation channel (pcc) family.
DR iPTMnet; Q8IZK6; -.
DR PhosphoSitePlus; Q8IZK6; -.
DR BioMuta; MCOLN2; -.
DR DMDM; 212276802; -.
DR MassIVE; Q8IZK6; -.
DR PaxDb; Q8IZK6; -.
DR PeptideAtlas; Q8IZK6; -.
DR PRIDE; Q8IZK6; -.
DR ProteomicsDB; 71363; -. [Q8IZK6-1]
DR ProteomicsDB; 71364; -. [Q8IZK6-2]
DR Antibodypedia; 19780; 46 antibodies from 12 providers.
DR DNASU; 255231; -.
DR Ensembl; ENST00000284027.5; ENSP00000284027.5; ENSG00000153898.13. [Q8IZK6-2]
DR Ensembl; ENST00000370608.8; ENSP00000359640.3; ENSG00000153898.13. [Q8IZK6-1]
DR GeneID; 255231; -.
DR KEGG; hsa:255231; -.
DR MANE-Select; ENST00000370608.8; ENSP00000359640.3; NM_153259.4; NP_694991.2.
DR UCSC; uc001dkm.4; human. [Q8IZK6-1]
DR CTD; 255231; -.
DR DisGeNET; 255231; -.
DR GeneCards; MCOLN2; -.
DR HGNC; HGNC:13357; MCOLN2.
DR HPA; ENSG00000153898; Tissue enhanced (intestine, lymphoid tissue).
DR MIM; 607399; gene.
DR neXtProt; NX_Q8IZK6; -.
DR OpenTargets; ENSG00000153898; -.
DR PharmGKB; PA134913691; -.
DR VEuPathDB; HostDB:ENSG00000153898; -.
DR eggNOG; KOG3733; Eukaryota.
DR GeneTree; ENSGT00950000183036; -.
DR HOGENOM; CLU_020945_1_1_1; -.
DR InParanoid; Q8IZK6; -.
DR OMA; HVCDADQ; -.
DR OrthoDB; 1379516at2759; -.
DR PhylomeDB; Q8IZK6; -.
DR TreeFam; TF317783; -.
DR PathwayCommons; Q8IZK6; -.
DR Reactome; R-HSA-3295583; TRP channels.
DR SignaLink; Q8IZK6; -.
DR BioGRID-ORCS; 255231; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; MCOLN2; human.
DR GeneWiki; MCOLN2; -.
DR GenomeRNAi; 255231; -.
DR Pharos; Q8IZK6; Tchem.
DR PRO; PR:Q8IZK6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8IZK6; protein.
DR Bgee; ENSG00000153898; Expressed in tibia and 124 other tissues.
DR ExpressionAtlas; Q8IZK6; baseline and differential.
DR Genevisible; Q8IZK6; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005262; F:calcium channel activity; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0072345; F:NAADP-sensitive calcium-release channel activity; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0070588; P:calcium ion transmembrane transport; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1905517; P:macrophage migration; IEA:Ensembl.
DR GO; GO:1990266; P:neutrophil migration; IEA:Ensembl.
DR GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; IEA:Ensembl.
DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IEA:Ensembl.
DR GO; GO:0071642; P:positive regulation of macrophage inflammatory protein 1 alpha production; IEA:Ensembl.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR039031; Mucolipin.
DR InterPro; IPR013122; PKD1_2_channel.
DR PANTHER; PTHR12127; PTHR12127; 1.
DR Pfam; PF08016; PKD_channel; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Calcium;
KW Calcium channel; Calcium transport; Cell membrane; Disulfide bond;
KW Endosome; Immunity; Innate immunity; Ion channel; Ion transport; Lysosome;
KW Membrane; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..566
FT /note="Mucolipin-2"
FT /id="PRO_0000215365"
FT TOPO_DOM 1..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT TOPO_DOM 87..288
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT TOPO_DOM 310..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT TOPO_DOM 368..376
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT TOPO_DOM 398..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT TOPO_DOM 441..448
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT INTRAMEM 449..469
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT TOPO_DOM 470..480
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT TRANSMEM 481..502
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT TOPO_DOM 503..566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT REGION 107..123
FT /note="Extracellular/lumenal pore loop"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU1"
FT MOTIF 461..464
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:F6RG56"
FT DISULFID 164..190
FT /evidence="ECO:0000250|UniProtKB:Q9GZU1"
FT DISULFID 243..274
FT /evidence="ECO:0000250|UniProtKB:Q9GZU1"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12403827"
FT /id="VSP_034642"
FT VARIANT 365
FT /note="M -> V (in dbSNP:rs17117841)"
FT /id="VAR_052394"
FT VARIANT 370
FT /note="K -> Q (in dbSNP:rs6704203)"
FT /id="VAR_052395"
FT MUTAGEN 424
FT /note="A->P: Constitutive active Ca(2+) permeable and
FT inward rectifying channel."
FT /evidence="ECO:0000269|PubMed:19940139"
FT MUTAGEN 457
FT /note="F->L: Does not effect current amplitude; possible
FT effect on regulation."
FT /evidence="ECO:0000269|PubMed:19940139"
FT MUTAGEN 463..464
FT /note="DD->KK: Blocks channel activity. Decreases recycling
FT of internalized CD59 to the cell surface."
FT /evidence="ECO:0000269|PubMed:17662026,
FT ECO:0000269|PubMed:19940139"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:6HRR"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:6HRR"
FT HELIX 124..139
FT /evidence="ECO:0007829|PDB:6HRR"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:6HRR"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:6HRR"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:6HRR"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:6HRR"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:6HRR"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6HRS"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:6HRR"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6HRR"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:6HRR"
FT STRAND 218..231
FT /evidence="ECO:0007829|PDB:6HRR"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:6HRS"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:6HRS"
FT STRAND 242..253
FT /evidence="ECO:0007829|PDB:6HRR"
FT STRAND 261..272
FT /evidence="ECO:0007829|PDB:6HRR"
SQ SEQUENCE 566 AA; 65942 MW; 6F017BA416624E63 CRC64;
MARQPYRFPQ ARIPERGSGV FRLTVRNAMA HRDSEMKEEC LREDLKFYFM SPCEKYRARR
QIPWKLGLQI LKIVMVTTQL VRFGLSNQLV VAFKEDNTVA FKHLFLKGYS GTDEDDYSCS
VYTQEDAYES IFFAINQYHQ LKDITLGTLG YGENEDNRIG LKVCKQHYKK GTMFPSNETL
NIDNDVELDC VQLDLQDLSK KPPDWKNSSF FRLEFYRLLQ VEISFHLKGI DLQTIHSREL
PDCYVFQNTI IFDNKAHSGK IKIYFDSDAK IEECKDLNIF GSTQKNAQYV LVFDAFVIVI
CLASLILCTR SIVLALRLRK RFLNFFLEKY KRPVCDTDQW EFINGWYVLV IISDLMTIIG
SILKMEIKAK NLTNYDLCSI FLGTSTLLVW VGVIRYLGYF QAYNVLILTM QASLPKVLRF
CACAGMIYLG YTFCGWIVLG PYHDKFENLN TVAECLFSLV NGDDMFATFA QIQQKSILVW
LFSRLYLYSF ISLFIYMILS LFIALITDSY DTIKKFQQNG FPETDLQEFL KECSSKEEYQ
KESSAFLSCI CCRRRKRSDD HLIPIS
