KCMB3_HUMAN
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 03-AUG-2022, entry version 161.
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}.
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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; DB01110; Miconazole.
DR DrugBank; DB00721; Procaine.
DR DrugBank; DB09089; Trimebutine.
DR TCDB; 8.A.14.1.4; the ca(2+)-activated k(+) channel auxiliary subunit slowpoke-Beta (sloBeta) family.
DR GlyGen; Q9NPA1; 1 site.
DR BioMuta; KCNMB3; -.
DR DMDM; 90111824; -.
DR MassIVE; Q9NPA1; -.
DR PaxDb; Q9NPA1; -.
DR PRIDE; Q9NPA1; -.
DR ProteomicsDB; 81947; -. [Q9NPA1-3]
DR ABCD; Q9NPA1; 1 sequenced antibody.
DR Antibodypedia; 3055; 287 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 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; DDWMDCA; -.
DR OrthoDB; 1178937at2759; -.
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 1082 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:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; PTHR10258; 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
