TTYH3_HUMAN
ID TTYH3_HUMAN Reviewed; 523 AA.
AC Q9C0H2; A4D201; B7WP98; Q6L749; Q6ZVG3; Q8TEG6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein tweety homolog 3;
DE Short=hTTY3;
GN Name=TTYH3; Synonyms=KIAA1691;
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 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, GLYCOSYLATION, GLYCOSYLATION AT ASN-351, TOPOLOGY, AND
RP MUTAGENESIS OF THR-128; THR-146; THR-353; ARG-367 AND HIS-370.
RX PubMed=15010458; DOI=10.1074/jbc.m313813200;
RA Suzuki M., Mizuno A.;
RT "A novel human Cl(-) channel family related to Drosophila flightless
RT locus.";
RL J. Biol. Chem. 279:22461-22468(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 342-523 (ISOFORM 4).
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 138-523 (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-144.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Probable large-conductance Ca(2+)-activated chloride channel.
CC May play a role in Ca(2+) signal transduction.
CC {ECO:0000269|PubMed:15010458}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15010458};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15010458}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9C0H2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0H2-2; Sequence=VSP_029770;
CC Name=3;
CC IsoId=Q9C0H2-3; Sequence=VSP_029769;
CC Name=4;
CC IsoId=Q9C0H2-4; Sequence=VSP_042220;
CC -!- TISSUE SPECIFICITY: Expressed in excitable tissues. Expressed in the
CC brain, heart, skeletal muscle, colon, spleen, kidney and peripheral
CC blood leukocytes. {ECO:0000269|PubMed:15010458}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15010458,
CC ECO:0000269|PubMed:19159218}.
CC -!- MISCELLANEOUS: The current is completely inhibited by the addition of
CC an anion permeability inhibitor. Addition of a Ca(2+) ionophore induces
CC an outward-rectified current in mock-transfected cells, but it
CC introduced an overt linear current in TTYH3-transfected cells.
CC -!- SIMILARITY: Belongs to the tweety family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21782.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EAL23958.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB162931; BAD20190.1; -; mRNA.
DR EMBL; AB051478; BAB21782.2; ALT_INIT; mRNA.
DR EMBL; AK124608; BAC85898.1; -; mRNA.
DR EMBL; AC006028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236953; EAL23958.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471144; EAW87266.1; -; Genomic_DNA.
DR EMBL; BC131824; AAI31825.1; -; mRNA.
DR EMBL; BC152447; AAI52448.1; -; mRNA.
DR EMBL; BE263005; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK074158; BAB84984.1; -; mRNA.
DR CCDS; CCDS34588.1; -. [Q9C0H2-1]
DR RefSeq; NP_079526.1; NM_025250.2. [Q9C0H2-1]
DR RefSeq; XP_011513837.1; XM_011515535.2. [Q9C0H2-4]
DR RefSeq; XP_016868145.1; XM_017012656.1. [Q9C0H2-2]
DR PDB; 7P5C; EM; 3.20 A; A/B=2-523.
DR PDBsum; 7P5C; -.
DR AlphaFoldDB; Q9C0H2; -.
DR SMR; Q9C0H2; -.
DR BioGRID; 123277; 160.
DR IntAct; Q9C0H2; 25.
DR STRING; 9606.ENSP00000258796; -.
DR TCDB; 1.A.48.1.4; the anion channel tweety (tweety) family.
DR GlyConnect; 1671; 2 N-Linked glycans (1 site).
DR GlyGen; Q9C0H2; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9C0H2; -.
DR PhosphoSitePlus; Q9C0H2; -.
DR SwissPalm; Q9C0H2; -.
DR BioMuta; TTYH3; -.
DR DMDM; 162416242; -.
DR EPD; Q9C0H2; -.
DR jPOST; Q9C0H2; -.
DR MassIVE; Q9C0H2; -.
DR MaxQB; Q9C0H2; -.
DR PaxDb; Q9C0H2; -.
DR PeptideAtlas; Q9C0H2; -.
DR PRIDE; Q9C0H2; -.
DR ProteomicsDB; 80038; -. [Q9C0H2-1]
DR ProteomicsDB; 80039; -. [Q9C0H2-2]
DR ProteomicsDB; 80040; -. [Q9C0H2-3]
DR ProteomicsDB; 80041; -. [Q9C0H2-4]
DR Antibodypedia; 43641; 26 antibodies from 11 providers.
DR DNASU; 80727; -.
DR Ensembl; ENST00000258796.12; ENSP00000258796.7; ENSG00000136295.15. [Q9C0H2-1]
DR Ensembl; ENST00000403167.5; ENSP00000385015.1; ENSG00000136295.15. [Q9C0H2-3]
DR Ensembl; ENST00000407643.5; ENSP00000385316.1; ENSG00000136295.15. [Q9C0H2-2]
DR GeneID; 80727; -.
DR KEGG; hsa:80727; -.
DR MANE-Select; ENST00000258796.12; ENSP00000258796.7; NM_025250.3; NP_079526.1.
DR UCSC; uc003smp.4; human. [Q9C0H2-1]
DR CTD; 80727; -.
DR DisGeNET; 80727; -.
DR GeneCards; TTYH3; -.
DR HGNC; HGNC:22222; TTYH3.
DR HPA; ENSG00000136295; Low tissue specificity.
DR MIM; 608919; gene.
DR neXtProt; NX_Q9C0H2; -.
DR OpenTargets; ENSG00000136295; -.
DR PharmGKB; PA134908427; -.
DR VEuPathDB; HostDB:ENSG00000136295; -.
DR eggNOG; KOG4433; Eukaryota.
DR GeneTree; ENSGT00950000183060; -.
DR HOGENOM; CLU_023758_0_1_1; -.
DR InParanoid; Q9C0H2; -.
DR OMA; PHTWQAR; -.
DR OrthoDB; 725378at2759; -.
DR PhylomeDB; Q9C0H2; -.
DR TreeFam; TF319025; -.
DR PathwayCommons; Q9C0H2; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR SignaLink; Q9C0H2; -.
DR BioGRID-ORCS; 80727; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; TTYH3; human.
DR GenomeRNAi; 80727; -.
DR Pharos; Q9C0H2; Tbio.
DR PRO; PR:Q9C0H2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9C0H2; protein.
DR Bgee; ENSG00000136295; Expressed in ventricular zone and 145 other tissues.
DR ExpressionAtlas; Q9C0H2; baseline and differential.
DR Genevisible; Q9C0H2; HS.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; IMP:UniProtKB.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IDA:FlyBase.
DR GO; GO:0072320; F:volume-sensitive chloride channel activity; IBA:GO_Central.
DR GO; GO:0006821; P:chloride transport; IDA:FlyBase.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR CDD; cd07912; Tweety_N; 1.
DR InterPro; IPR006990; Tweety.
DR PANTHER; PTHR12424; PTHR12424; 1.
DR Pfam; PF04906; Tweety; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane; Chloride;
KW Chloride channel; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..523
FT /note="Protein tweety homolog 3"
FT /id="PRO_0000312251"
FT TOPO_DOM 1..42
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..386
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 413..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P5F7"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P5F7"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:15010458"
FT VAR_SEQ 1..208
FT /note="MAGVSYAAPWWVSLLHRLPHFDLSWEATSSQFRPEDTDYQQALLLLGAAALA
FT CLALDLLFLLFYSFWLCCRRRKSEEHLDADCCCTAWCVIIATLVCSAGIAVGFYGNGET
FT SDGIHRATYSLRHANRTVAGVQDRVWDTAVGLNHTAEPSLQTLERQLAGRPEPLRAVQR
FT LQGLLETLLGYTAAIPFWRNTAVSLEVLAEQVDLYDWY -> MPSGVPGCWPQLPLKGP
FT WRPTPRPRVPVPWRTPRFAC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029769"
FT VAR_SEQ 210..241
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_029770"
FT VAR_SEQ 501..523
FT /note="YTSSMRAKYLATSQPRPDSSGSH -> RYLAALDSGSHAGWQFKPMDSARTL
FT W (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042220"
FT MUTAGEN 128
FT /note="T->A: Does not affect N-glycosylation state."
FT /evidence="ECO:0000269|PubMed:15010458"
FT MUTAGEN 146
FT /note="T->A: Does not affect N-glycosylation state."
FT /evidence="ECO:0000269|PubMed:15010458"
FT MUTAGEN 353
FT /note="T->A: Abolishes N-glycosylation."
FT /evidence="ECO:0000269|PubMed:15010458"
FT MUTAGEN 367
FT /note="R->Q: Induces a stronger permeability to cations."
FT /evidence="ECO:0000269|PubMed:15010458"
FT MUTAGEN 370
FT /note="H->D: Shows a different ion selectivity."
FT /evidence="ECO:0000269|PubMed:15010458"
FT CONFLICT 169
FT /note="Q -> K (in Ref. 9; BAB84984)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="V -> F (in Ref. 8; BE263005)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="S -> R (in Ref. 9; BAB84984)"
FT /evidence="ECO:0000305"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:7P5C"
FT HELIX 37..65
FT /evidence="ECO:0007829|PDB:7P5C"
FT HELIX 88..157
FT /evidence="ECO:0007829|PDB:7P5C"
FT HELIX 162..184
FT /evidence="ECO:0007829|PDB:7P5C"
FT HELIX 195..233
FT /evidence="ECO:0007829|PDB:7P5C"
FT HELIX 236..272
FT /evidence="ECO:0007829|PDB:7P5C"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:7P5C"
FT HELIX 290..298
FT /evidence="ECO:0007829|PDB:7P5C"
FT HELIX 308..335
FT /evidence="ECO:0007829|PDB:7P5C"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:7P5C"
FT HELIX 340..363
FT /evidence="ECO:0007829|PDB:7P5C"
FT HELIX 366..408
FT /evidence="ECO:0007829|PDB:7P5C"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:7P5C"
SQ SEQUENCE 523 AA; 57545 MW; B398391787BA0301 CRC64;
MAGVSYAAPW WVSLLHRLPH FDLSWEATSS QFRPEDTDYQ QALLLLGAAA LACLALDLLF
LLFYSFWLCC RRRKSEEHLD ADCCCTAWCV IIATLVCSAG IAVGFYGNGE TSDGIHRATY
SLRHANRTVA GVQDRVWDTA VGLNHTAEPS LQTLERQLAG RPEPLRAVQR LQGLLETLLG
YTAAIPFWRN TAVSLEVLAE QVDLYDWYRW LGYLGLLLLD VIICLLVLVG LIRSSKGILV
GVCLLGVLAL VISWGALGLE LAVSVGSSDF CVDPDAYVTK MVEEYSVLSG DILQYYLACS
PRAANPFQQK LSGSHKALVE MQDVVAELLR TVPWEQPATK DPLLRVQEVL NGTEVNLQHL
TALVDCRSLH LDYVQALTGF CYDGVEGLIY LALFSFVTAL MFSSIVCSVP HTWQQKRGPD
EDGEEEAAPG PRQAHDSLYR VHMPSLYSCG SSYGSETSIP AAAHTVSNAP VTEYMSQNAN
FQNPRCENTP LIGRESPPPS YTSSMRAKYL ATSQPRPDSS GSH
