CLD10_MOUSE
ID CLD10_MOUSE Reviewed; 231 AA.
AC Q9Z0S6; E9PVC8; E9PWP4; E9QMP1; Q8VC62; Q9CX57;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Claudin-10;
GN Name=Cldn10; Synonyms=Cldn10a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Morita K., Furuse M., Tsukita S.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ISOFORM 2.
RX PubMed=16804102; DOI=10.1152/ajprenal.00138.2006;
RA Van Itallie C.M., Rogan S., Yu A., Vidal L.S., Holmes J., Anderson J.M.;
RT "Two splice variants of claudin-10 in the kidney create paracellular pores
RT with different ion selectivities.";
RL Am. J. Physiol. 291:F1288-F1299(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), FUNCTION,
RP SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DOMAIN.
RC TISSUE=Kidney;
RX PubMed=19383724; DOI=10.1242/jcs.040113;
RA Gunzel D., Stuiver M., Kausalya P.J., Haisch L., Krug S.M., Rosenthal R.,
RA Meij I.C., Hunziker W., Fromm M., Muller D.;
RT "Claudin-10 exists in six alternatively spliced isoforms that exhibit
RT distinct localization and function.";
RL J. Cell Sci. 122:1507-1517(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=FVB/N; TISSUE=Kidney, and Mammary gland;
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=14698084; DOI=10.1016/s0378-5955(03)00338-1;
RA Kitajiri S.I., Furuse M., Morita K., Saishin-Kiuchi Y., Kido H., Ito J.,
RA Tsukita S.;
RT "Expression patterns of claudins, tight junction adhesion molecules, in the
RT inner ear.";
RL Hear. Res. 187:25-34(2004).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=16520537; DOI=10.1292/jvms.68.149;
RA Ohta H., Adachi H., Inaba M.;
RT "Developmental changes in the expression of tight junction protein claudins
RT in murine metanephroi and embryonic kidneys.";
RL J. Vet. Med. Sci. 68:149-155(2006).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=17075866; DOI=10.1002/dvdy.21001;
RA Ohazama A., Sharpe P.T.;
RT "Expression of claudins in murine tooth development.";
RL Dev. Dyn. 236:290-294(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22891322; DOI=10.1073/pnas.1203834109;
RA Breiderhoff T., Himmerkus N., Stuiver M., Mutig K., Will C., Meij I.C.,
RA Bachmann S., Bleich M., Willnow T.E., Muller D.;
RT "Deletion of claudin-10 (Cldn10) in the thick ascending limb impairs
RT paracellular sodium permeability and leads to hypermagnesemia and
RT nephrocalcinosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:14241-14246(2012).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=28771254; DOI=10.1038/gim.2017.71;
RA Hadj-Rabia S., Brideau G., Al-Sarraj Y., Maroun R.C., Figueres M.L.,
RA Leclerc-Mercier S., Olinger E., Baron S., Chaussain C., Nochy D.,
RA Taha R.Z., Knebelmann B., Joshi V., Curmi P.A., Kambouris M.,
RA Vargas-Poussou R., Bodemer C., Devuyst O., Houillier P., El-Shanti H.;
RT "Multiplex epithelium dysfunction due to CLDN10 mutation: the HELIX
RT syndrome.";
RL Genet. Med. 20:190-201(2018).
CC -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC the intercellular space, through calcium-independent cell-adhesion
CC activity. Involved in the regulation of paracellular epithelia
CC permeability to ions in multiple organs. It acts as a paracellular ion
CC channel probably forming permselective pores; isoform 1 appears to
CC create pores preferentially permeable to cations and isoform 2 for
CC anions. In sweat glands and in the thick ascending limb (TAL) of
CC Henle's loop in kidney, it controls paracellular sodium permeability
CC which is essential for proper sweat production and renal function.
CC {ECO:0000250|UniProtKB:P78369, ECO:0000269|PubMed:16804102,
CC ECO:0000269|PubMed:19383724, ECO:0000269|PubMed:22891322}.
CC -!- SUBUNIT: Can form homodimers both in trans (interaction between CLDN10
CC molecules in opposing membranes) and in cis (interaction between CLDN10
CC molecules within one membrane). {ECO:0000250|UniProtKB:P78369}.
CC -!- INTERACTION:
CC Q9Z0S6; Q8N6F1-2: CLDN19; Xeno; NbExp=2; IntAct=EBI-15799971, EBI-12256978;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:16804102, ECO:0000269|PubMed:19383724}. Cell
CC membrane {ECO:0000269|PubMed:19383724}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:19383724}.
CC Note=Isoform 1, isoform 2 and isoform 4 localize in the cell membrane
CC and at epithelial tight junctions, whereas isoform 3, isoform 5 and
CC isoform 6 are detected in the endoplasmic reticulum.
CC {ECO:0000269|PubMed:19383724}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Cldn10b;
CC IsoId=Q9Z0S6-1; Sequence=Displayed;
CC Name=2; Synonyms=Cldn10a;
CC IsoId=Q9Z0S6-2; Sequence=VSP_053551;
CC Name=3; Synonyms=Cldn10a_i2;
CC IsoId=Q9Z0S6-3; Sequence=VSP_053551, VSP_053553;
CC Name=4; Synonyms=Cldn10a_i1;
CC IsoId=Q9Z0S6-4; Sequence=VSP_053552;
CC Name=5; Synonyms=Cldn10a_i3;
CC IsoId=Q9Z0S6-5; Sequence=VSP_053552, VSP_053553;
CC Name=6; Synonyms=Cldn10b_i1;
CC IsoId=Q9Z0S6-6; Sequence=VSP_053553;
CC -!- TISSUE SPECIFICITY: Strong expression detected in brain cortex and
CC kidney and weak expression in lung and cecum. In kidney, detected in
CC thick ascending limb (TAL) of Henle's loop and proximal convoluted
CC tubule (PCT). Isoform 1 is widely expressed, with highest expression
CC detected in brain cortex, kidney and lung. Isoform 2, isoform 3,
CC isoform 4 and isoform 5 are only detected in kidney and uterus. In
CC kidney, the expression of isoform 1 is highest in medulla, with
CC transcripts being detected in medullary thick ascending limb of Henle's
CC loop (mTAL) and outer and inner medullary collecting ducts, whereas
CC isoform 2 (along with isoform 4) is more highly expressed in cortex,
CC with transcripts being detected in PCT, mTAL and cortical collecting
CC duct. Expressed in the inner ear where it is detected in organ of
CC Corti, marginal cells of stria vascularis, Reissner's membrane and
CC spiral limbus (at protein level) (PubMed:14698084). Expressed in
CC salivary glands and skin (PubMed:28771254).
CC {ECO:0000269|PubMed:14698084, ECO:0000269|PubMed:16804102,
CC ECO:0000269|PubMed:19383724, ECO:0000269|PubMed:22891322,
CC ECO:0000269|PubMed:28771254}.
CC -!- DEVELOPMENTAL STAGE: Detected in developing kidney at 14 dpc, with
CC levels increasing towards adulthood. Expressed during tooth
CC development: at 12 dpc, detected in the thickening tooth epithelium, at
CC 13.5 dpc in the lingual basal epithelium of the bud epithelium, at 14.5
CC dpc in lingual epithelium and between 18 dpc to postnatal day 1 in
CC odontoblasts and stratum intermedium. {ECO:0000269|PubMed:16520537,
CC ECO:0000269|PubMed:17075866}.
CC -!- DOMAIN: The fourth transmembrane region (161-181), which is missing in
CC isoform 3, isoform 5 and isoform 6, is necessary for integration into
CC tight junctions. {ECO:0000269|PubMed:19383724}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout in the thick ascending limb
CC (TAL) of Henle's loop in kidney leads to hypocalcemia, hypermagnesemia,
CC hyperphosphatemia and nephrocalcinosis. {ECO:0000269|PubMed:22891322}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform
CC 2. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing of isoform
CC 3. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; AF124425; AAD17320.1; -; mRNA.
DR EMBL; AK020131; BAB32005.1; -; mRNA.
DR EMBL; AC154377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT025524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021770; AAH21770.1; -; mRNA.
DR EMBL; BC029019; AAH29019.1; -; mRNA.
DR CCDS; CCDS37009.1; -. [Q9Z0S6-2]
DR CCDS; CCDS37010.1; -. [Q9Z0S6-1]
DR CCDS; CCDS49566.1; -. [Q9Z0S6-3]
DR RefSeq; NP_001153568.1; NM_001160096.1. [Q9Z0S6-4]
DR RefSeq; NP_001153569.1; NM_001160097.1. [Q9Z0S6-3]
DR RefSeq; NP_001153570.1; NM_001160098.1. [Q9Z0S6-5]
DR RefSeq; NP_001153571.1; NM_001160099.1. [Q9Z0S6-6]
DR RefSeq; NP_067361.2; NM_021386.4. [Q9Z0S6-1]
DR RefSeq; NP_076367.2; NM_023878.3. [Q9Z0S6-2]
DR AlphaFoldDB; Q9Z0S6; -.
DR SMR; Q9Z0S6; -.
DR DIP; DIP-48952N; -.
DR DIP; DIP-48954N; -.
DR IntAct; Q9Z0S6; 4.
DR STRING; 10090.ENSMUSP00000097889; -.
DR TCDB; 1.H.1.1.10; the claudin tight junction (claudin1) family.
DR iPTMnet; Q9Z0S6; -.
DR PhosphoSitePlus; Q9Z0S6; -.
DR PaxDb; Q9Z0S6; -.
DR PRIDE; Q9Z0S6; -.
DR ProteomicsDB; 283283; -. [Q9Z0S6-1]
DR ProteomicsDB; 283284; -. [Q9Z0S6-2]
DR ProteomicsDB; 283285; -. [Q9Z0S6-3]
DR ProteomicsDB; 283286; -. [Q9Z0S6-4]
DR ProteomicsDB; 283287; -. [Q9Z0S6-5]
DR ProteomicsDB; 283288; -. [Q9Z0S6-6]
DR Antibodypedia; 4562; 274 antibodies from 32 providers.
DR DNASU; 58187; -.
DR Ensembl; ENSMUST00000047761; ENSMUSP00000041616; ENSMUSG00000022132. [Q9Z0S6-2]
DR Ensembl; ENSMUST00000071546; ENSMUSP00000071476; ENSMUSG00000022132. [Q9Z0S6-3]
DR Ensembl; ENSMUST00000100314; ENSMUSP00000097889; ENSMUSG00000022132. [Q9Z0S6-1]
DR GeneID; 58187; -.
DR KEGG; mmu:58187; -.
DR UCSC; uc007uyw.2; mouse. [Q9Z0S6-2]
DR UCSC; uc007uyx.2; mouse. [Q9Z0S6-1]
DR UCSC; uc011zqb.1; mouse. [Q9Z0S6-4]
DR UCSC; uc011zqc.1; mouse. [Q9Z0S6-5]
DR UCSC; uc011zqd.1; mouse. [Q9Z0S6-3]
DR UCSC; uc011zqe.1; mouse. [Q9Z0S6-6]
DR CTD; 9071; -.
DR MGI; MGI:1913101; Cldn10.
DR VEuPathDB; HostDB:ENSMUSG00000022132; -.
DR eggNOG; ENOG502QPNP; Eukaryota.
DR GeneTree; ENSGT00940000155232; -.
DR HOGENOM; CLU_076370_0_0_1; -.
DR InParanoid; Q9Z0S6; -.
DR OMA; CKEFISM; -.
DR OrthoDB; 1164514at2759; -.
DR PhylomeDB; Q9Z0S6; -.
DR TreeFam; TF331936; -.
DR BioGRID-ORCS; 58187; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Cldn10; mouse.
DR PRO; PR:Q9Z0S6; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9Z0S6; protein.
DR Bgee; ENSMUSG00000022132; Expressed in right kidney and 160 other tissues.
DR Genevisible; Q9Z0S6; MM.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0070830; P:bicellular tight junction assembly; IBA:GO_Central.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0043269; P:regulation of ion transport; ISS:UniProtKB.
DR InterPro; IPR006187; Claudin.
DR InterPro; IPR003554; Claudin10.
DR InterPro; IPR017974; Claudin_CS.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR PANTHER; PTHR12002; PTHR12002; 1.
DR PANTHER; PTHR12002:SF13; PTHR12002:SF13; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01383; CLAUDIN10.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Endoplasmic reticulum;
KW Ion transport; Membrane; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..231
FT /note="Claudin-10"
FT /id="PRO_0000144758"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..80
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..73
FT /note="MASTALEIVAFVVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYFANLWKI
FT CVTDSTGVANCKEFPSMLALD -> MSRAQISALVCGVGGFGALVAATTSNEWKVTTRA
FT SSVITATWVYQGLWMNCAGNALGSFHCRPHFTIFKVE (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:16804102,
FT ECO:0000303|PubMed:19383724"
FT /id="VSP_053551"
FT VAR_SEQ 1..73
FT /note="MASTALEIVAFVVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYFANLWKI
FT CVTDSTGVANCKEFPSMLALD -> MSRAQISALVCGVGGFGALVAATTSNEWKVTTRA
FT SSVITATWVYQGLWMNCA (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:19383724"
FT /id="VSP_053552"
FT VAR_SEQ 156..191
FT /note="Missing (in isoform 3, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:19383724"
FT /id="VSP_053553"
FT CONFLICT 104
FT /note="T -> S (in Ref. 1; BAB32005)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="A -> V (in Ref. 1; AAD17320 and 6; AAH21770/
FT AAH29019)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="T -> A (in Ref. 1; AAD17320, 6; AAH21770/AAH29019
FT and 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 24695 MW; 80A28863B258DED2 CRC64;
MASTALEIVA FVVSISGWVL VSSTLPTDYW KVSTIDGTVI TTATYFANLW KICVTDSTGV
ANCKEFPSML ALDGYIQACR GLMIAAVSLG FFGSIFALFG MKCTKVGGSD QAKAKIACLA
GIVFILSGLC SMTGCSLYAN KITTEFFDPL YMEQKYELGA ALFIGWAGAS LCIIGGVIFC
FSISDNNKTP RMGYTYNGPT SAMSSRTKYQ GGEGDFKTTG PSKQFDKNAY V
