ID KCMB3_HUMAN Reviewed; 279 AA. AC Q9NPA1; B7Z9C9; D3DNR2; E9PER5; Q9NPG7; Q9NRM9; Q9UHN3; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 2. DT 08-NOV-2023, entry version 168. DE RecName: Full=Calcium-activated potassium channel subunit beta-3; DE AltName: Full=BK channel subunit beta-3; DE Short=BKbeta3; DE Short=Hbeta3; DE AltName: Full=Calcium-activated potassium channel, subfamily M subunit beta-3; DE AltName: Full=Charybdotoxin receptor subunit beta-3; DE AltName: Full=K(VCA)beta-3; DE AltName: Full=Maxi K channel subunit beta-3; DE AltName: Full=Slo-beta-3; GN Name=KCNMB3; Synonyms=KCNMB2, KCNMBL; 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 3), VARIANT THR-53, AND TISSUE RP SPECIFICITY. RX PubMed=10585773; DOI=10.1006/geno.1999.5975; RA Riazi M.A., Brinkman-Mills P., Johnson A., Naylor S.L., Minoshima S., RA Shimizu N., Baldini A., McDermid H.E.; RT "Identification of a putative regulatory subunit of a calcium-activated RT potassium channel in the dup(3q) syndrome region and a related sequence on RT 22q11.2."; RL Genomics 62:90-94(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT THR-53, TISSUE SPECIFICITY, RP AND INTERACTION WITH KCNMA1. RC TISSUE=Brain; RX PubMed=10692449; DOI=10.1074/jbc.275.9.6453; RA Brenner R., Jegla T.J., Wickenden A., Liu Y., Aldrich R.W.; RT "Cloning and functional characterization of novel large conductance RT calcium-activated potassium channel beta subunits, hKCNMB3 and hKCNMB4."; RL J. Biol. Chem. 275:6453-6461(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND VARIANTS THR-53 AND SER-165. RC TISSUE=Spleen; RX PubMed=10766764; DOI=10.1074/jbc.m910187199; RA Uebele V.N., Lagrutta A.A., Wade T., Figueroa D.J., Liu Y., McKenna E., RA Austin C.P., Bennett P.B., Swanson R.; RT "Cloning and functional expression of two families of Beta-subunits of the RT large conductance calcium-activated potassium channel."; RL J. Biol. Chem. 275:23211-23218(2000). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-53, AND GLYCOSYLATION. RX PubMed=10792058; DOI=10.1073/pnas.100118597; RA Meera P., Wallner M., Toro L.; RT "A neuronal beta subunit (KCNMB4) makes the large conductance, voltage- and RT Ca2+-activated K+ channel resistant to charybdotoxin and iberiotoxin."; RL Proc. Natl. Acad. Sci. U.S.A. 97:5562-5567(2000). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT THR-53. RX PubMed=10828459; DOI=10.1016/s0014-5793(00)01584-2; RA Behrens R., Nolting A., Reimann F., Schwarz M., Waldschuetz R., Pongs O.; RT "hKCNMB3 and hKCNMB4, cloning and characterization of two members of the RT large-conductance calcium-activated potassium channel beta subunit RT family."; RL FEBS Lett. 474:99-106(2000). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [8] 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 [9] RP FUNCTION. RX PubMed=10864947; DOI=10.1523/jneurosci.20-13-04890.2000; RA Xia X.-M., Ding J.-P., Zeng X.-H., Duan K.-L., Lingle C.J.; RT "Rectification and rapid activation at low Ca2+ of Ca2+-activated, voltage- RT dependent BK currents: consequences of rapid inactivation by a novel beta RT subunit."; RL J. Neurosci. 20:4890-4903(2000). RN [10] RP DOMAIN. RX PubMed=11382808; DOI=10.1085/jgp.117.6.583; RA Lingle C.J., Zeng X.-H., Ding J.-P., Xia X.-M.; RT "Inactivation of BK channels mediated by the NH(2) terminus of the beta3b RT auxiliary subunit involves a two-step mechanism: possible separation of RT binding and blockade."; RL J. Gen. Physiol. 117:583-606(2001). RN [11] RP DOMAIN. RX PubMed=11382809; DOI=10.1085/jgp.117.6.607; RA Zeng X.-H., Ding J.-P., Xia X.-M., Lingle C.J.; RT "Gating properties conferred on BK channels by the beta3b auxiliary subunit RT in the absence of its NH(2)- and COOH termini."; RL J. Gen. Physiol. 117:607-628(2001). RN [12] RP VARIANTS VAL-75; SER-165 AND THR-230. RX PubMed=14612589; DOI=10.1152/physiolgenomics.00110.2003; RA Hu S., Labuda M.Z., Pandolfo M., Goss G.G., McDermid H.E., Ali D.W.; RT "Variants of the KCNMB3 regulatory subunit of maxi BK channels affect RT channel inactivation."; RL Physiol. Genomics 15:191-198(2003). RN [13] RP DISULFIDE BONDS, AND DOMAIN. RX PubMed=12740608; DOI=10.1038/nsb932; RA Zeng X.-H., Xia X.-M., Lingle C.J.; RT "Redox-sensitive extracellular gates formed by auxiliary beta subunits of RT calcium-activated potassium channels."; RL Nat. Struct. Biol. 10:448-454(2003). RN [14] RP REVIEW. RX PubMed=12136044; DOI=10.1152/nips.01387.2002; RA Orio P., Rojas P., Ferreira G., Latorre R.; RT "New disguises for an old channel: MaxiK channel beta-subunits."; RL News Physiol. Sci. 17:156-161(2002). CC -!- FUNCTION: Regulatory subunit of the calcium activated potassium KCNMA1 CC (maxiK) channel. Modulates the calcium sensitivity and gating kinetics CC of KCNMA1, thereby contributing to KCNMA1 channel diversity. Alters the CC functional properties of the current expressed by the KCNMA1 channel. CC Isoform 2, isoform 3 and isoform 4 partially inactivate the current of CC KCNBMA. Isoform 4 induces a fast and incomplete inactivation of KCNMA1 CC channel that is detectable only at large depolarizations. In contrast, CC isoform 1 does not induce detectable inactivation of KCNMA1. Two or CC more subunits of KCNMB3 are required to block the KCNMA1 tetramer. CC {ECO:0000269|PubMed:10766764, ECO:0000269|PubMed:10864947}. CC -!- SUBUNIT: Interacts with KCNMA1 tetramer. There are probably 4 molecules CC of KCMNB3 per KCNMA1 tetramer. {ECO:0000269|PubMed:10692449}. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=3d; CC IsoId=Q9NPA1-1; Sequence=Displayed; CC Name=2; Synonyms=3a; CC IsoId=Q9NPA1-2; Sequence=VSP_009827; CC Name=3; Synonyms=3c; CC IsoId=Q9NPA1-3; Sequence=VSP_009828; CC Name=4; Synonyms=3b; CC IsoId=Q9NPA1-4; Sequence=VSP_009829, VSP_009830; CC Name=5; CC IsoId=Q9NPA1-5; Sequence=VSP_009827, VSP_046090, VSP_046091; CC -!- TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 4 are widely CC expressed. Isoform 2 is expressed placenta, pancreas, kidney and heart. CC Isoform 1 and isoform 3 are highly expressed in pancreas and testis. CC {ECO:0000269|PubMed:10585773, ECO:0000269|PubMed:10692449, CC ECO:0000269|PubMed:10766764}. CC -!- DOMAIN: Isoform 4 cytoplasmic N-terminal domain participates in the CC partial inactivation of KCNMA1, possibly by binding to a receptor site. CC -!- DOMAIN: The extracellular domain forms gates to block ion permeation, CC providing a mechanism by which current can be rapidly diminished upon CC cellular repolarization. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10792058}. CC -!- PTM: The extracellular domain contains disulfide bond essential for the CC gating mechanism. CC -!- SIMILARITY: Belongs to the KCNMB (TC 8.A.14.1) family. KCNMB3 CC subfamily. {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; AF139471; AAD54771.1; -; mRNA. DR EMBL; AF214561; AAF36598.1; -; mRNA. DR EMBL; AF204159; AAF97031.1; -; Genomic_DNA. DR EMBL; AF204160; AAF97032.1; -; Genomic_DNA. DR EMBL; AF204161; AAF97033.1; -; Genomic_DNA. DR EMBL; AF204162; AAF97034.1; -; Genomic_DNA. DR EMBL; AF160968; AAF67811.1; -; mRNA. DR EMBL; AF170916; AAF89698.1; -; mRNA. DR EMBL; AK304837; BAH14265.1; -; mRNA. DR EMBL; AC007823; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC076966; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW78418.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78421.1; -; Genomic_DNA. DR CCDS; CCDS3225.1; -. [Q9NPA1-2] DR CCDS; CCDS3226.1; -. [Q9NPA1-1] DR CCDS; CCDS43172.1; -. [Q9NPA1-4] DR CCDS; CCDS43173.1; -. [Q9NPA1-3] DR CCDS; CCDS54683.1; -. [Q9NPA1-5] DR RefSeq; NP_001157149.1; NM_001163677.1. [Q9NPA1-5] DR RefSeq; NP_055222.3; NM_014407.3. [Q9NPA1-1] DR RefSeq; NP_741979.1; NM_171828.2. [Q9NPA1-2] DR RefSeq; NP_741980.1; NM_171829.2. [Q9NPA1-4] DR RefSeq; NP_741981.1; NM_171830.1. [Q9NPA1-3] DR AlphaFoldDB; Q9NPA1; -. DR SMR; Q9NPA1; -. DR BioGRID; 117996; 54. DR STRING; 9606.ENSP00000319370; -. DR DrugBank; DB02587; Colforsin. DR DrugBank; DB01110; Miconazole. DR DrugBank; DB01054; Nitrendipine. DR DrugBank; DB00721; Procaine. DR DrugBank; DB00867; Ritodrine. DR DrugBank; DB09089; Trimebutine. DR TCDB; 8.A.14.1.4; the ca(2+)-activated k(+) channel auxiliary subunit slowpoke-Beta (sloBeta) family. DR GlyCosmos; Q9NPA1; 1 site, No reported glycans. DR GlyGen; Q9NPA1; 1 site. DR BioMuta; KCNMB3; -. DR DMDM; 90111824; -. DR MassIVE; Q9NPA1; -. DR PaxDb; 9606-ENSP00000319370; -. DR PeptideAtlas; Q9NPA1; -. DR ABCD; Q9NPA1; 1 sequenced antibody. DR Antibodypedia; 3055; 300 antibodies from 32 providers. DR DNASU; 27094; -. DR Ensembl; ENST00000314235.9; ENSP00000319370.5; ENSG00000171121.17. [Q9NPA1-1] DR Ensembl; ENST00000349697.2; ENSP00000327866.2; ENSG00000171121.17. [Q9NPA1-2] DR Ensembl; ENST00000392685.7; ENSP00000376451.2; ENSG00000171121.17. [Q9NPA1-3] DR Ensembl; ENST00000392686.6; ENSP00000376452.2; ENSG00000171121.17. [Q9NPA1-4] DR Ensembl; ENST00000485523.5; ENSP00000418536.1; ENSG00000171121.17. [Q9NPA1-4] DR Ensembl; ENST00000497599.5; ENSP00000417091.1; ENSG00000171121.17. [Q9NPA1-5] DR GeneID; 27094; -. DR KEGG; hsa:27094; -. DR MANE-Select; ENST00000392685.7; ENSP00000376451.2; NM_171830.2; NP_741981.1. [Q9NPA1-3] DR UCSC; uc003fjm.4; human. [Q9NPA1-1] DR AGR; HGNC:6287; -. DR CTD; 27094; -. DR DisGeNET; 27094; -. DR GeneCards; KCNMB3; -. DR HGNC; HGNC:6287; KCNMB3. DR HPA; ENSG00000171121; Low tissue specificity. DR MIM; 605222; gene. DR neXtProt; NX_Q9NPA1; -. DR OpenTargets; ENSG00000171121; -. DR PharmGKB; PA30067; -. DR VEuPathDB; HostDB:ENSG00000171121; -. DR eggNOG; ENOG502QR4Z; Eukaryota. DR GeneTree; ENSGT00950000183039; -. DR HOGENOM; CLU_085739_1_0_1; -. DR InParanoid; Q9NPA1; -. DR OMA; ESNCTVI; -. DR OrthoDB; 4267391at2759; -. DR PhylomeDB; Q9NPA1; -. DR TreeFam; TF328589; -. DR PathwayCommons; Q9NPA1; -. DR Reactome; R-HSA-1296052; Ca2+ activated K+ channels. DR Reactome; R-HSA-418457; cGMP effects. DR BioGRID-ORCS; 27094; 12 hits in 1165 CRISPR screens. DR ChiTaRS; KCNMB3; human. DR GeneWiki; KCNMB3; -. DR GenomeRNAi; 27094; -. DR Pharos; Q9NPA1; Tbio. DR PRO; PR:Q9NPA1; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9NPA1; Protein. DR Bgee; ENSG00000171121; Expressed in primary visual cortex and 96 other tissues. DR ExpressionAtlas; Q9NPA1; baseline and differential. DR Genevisible; Q9NPA1; HS. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB. DR GO; GO:0015269; F:calcium-activated potassium channel activity; IDA:UniProtKB. DR GO; GO:0015459; F:potassium channel regulator activity; IBA:GO_Central. DR GO; GO:0001508; P:action potential; IDA:UniProtKB. DR GO; GO:0005513; P:detection of calcium ion; IDA:UniProtKB. DR GO; GO:0019228; P:neuronal action potential; IDA:UniProtKB. DR GO; GO:0006813; P:potassium ion transport; IDA:UniProtKB. DR InterPro; IPR003930; K_chnl_Ca-activ_BK_bsu. DR PANTHER; PTHR10258; CALCIUM-ACTIVATED POTASSIUM CHANNEL SUBUNIT BETA; 1. DR PANTHER; PTHR10258:SF4; CALCIUM-ACTIVATED POTASSIUM CHANNEL SUBUNIT BETA-3; 1. DR Pfam; PF03185; CaKB; 1. PE 1: Evidence at protein level; KW Alternative splicing; Disulfide bond; Glycoprotein; Ion channel; KW Ion transport; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..279 FT /note="Calcium-activated potassium channel subunit beta-3" FT /id="PRO_0000187054" FT TOPO_DOM 1..60 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 61..81 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 82..207 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 208..228 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 229..279 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 131 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..22 FT /note="MDFSPSSELGFHFVAFILLTRH -> MQPFSIPVQITLQGSRRRQG (in FT isoform 2 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_009827" FT VAR_SEQ 1..22 FT /note="MDFSPSSELGFHFVAFILLTRH -> MFPLLYELTAVSPSPFPQ (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:10585773" FT /id="VSP_009828" FT VAR_SEQ 1..22 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10692449, FT ECO:0000303|PubMed:10828459" FT /id="VSP_009829" FT VAR_SEQ 23 FT /note="R -> M (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10692449, FT ECO:0000303|PubMed:10828459" FT /id="VSP_009830" FT VAR_SEQ 154..175 FT /note="CFYTPKCHQDRNDLLNSALDIK -> RDVTDCRVKEKQTLTVSDEHKQ (in FT isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046090" FT VAR_SEQ 176..279 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046091" FT VARIANT 44 FT /note="D -> G (in dbSNP:rs1170672)" FT /id="VAR_018173" FT VARIANT 53 FT /note="A -> T (in dbSNP:rs7645550)" FT /evidence="ECO:0000269|PubMed:10585773, FT ECO:0000269|PubMed:10692449, ECO:0000269|PubMed:10766764, FT ECO:0000269|PubMed:10792058, ECO:0000269|PubMed:10828459" FT /id="VAR_018174" FT VARIANT 75 FT /note="L -> V (in dbSNP:rs2276802)" FT /evidence="ECO:0000269|PubMed:14612589" FT /id="VAR_018175" FT VARIANT 165 FT /note="N -> S (in dbSNP:rs55710741)" FT /evidence="ECO:0000269|PubMed:10766764, FT ECO:0000269|PubMed:14612589" FT /id="VAR_018176" FT VARIANT 230 FT /note="M -> T (in dbSNP:rs145985409)" FT /evidence="ECO:0000269|PubMed:14612589" FT /id="VAR_018177" FT CONFLICT 24 FT /note="T -> P (in Ref. 6; BAH14265)" FT /evidence="ECO:0000305" SQ SEQUENCE 279 AA; 31604 MW; EC5F0D5D3E040C4C CRC64; MDFSPSSELG FHFVAFILLT RHRTAFPASG KKRETDYSDG DPLDVHKRLP SSAGEDRAVM LGFAMMGFSV LMFFLLGTTI LKPFMLSIQR EESTCTAIHT DIMDDWLDCA FTCGVHCHGQ GKYPCLQVFV NLSHPGQKAL LHYNEEAVQI NPKCFYTPKC HQDRNDLLNS ALDIKEFFDH KNGTPFSCFY SPASQSEDVI LIKKYDQMAI FHCLFWPSLT LLGGALIVGM VRLTQHLSLL CEKYSTVVRD EVGGKVPYIE QHQFKLCIMR RSKGRAEKS //