TXND9_HUMAN
ID TXND9_HUMAN Reviewed; 226 AA.
AC O14530; B2R9G8; D3DVI4; Q53HG4; Q53RV8; Q6NSF5; Q8TB70; Q9BRU6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Thioredoxin domain-containing protein 9;
DE AltName: Full=ATP-binding protein associated with cell differentiation;
DE AltName: Full=Protein 1-4;
GN Name=TXNDC9; Synonyms=APACD;
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).
RC TISSUE=Leukemia;
RA Shiosaka T.;
RT "Differential expression of 1-4 gene in functionally distinct ME-1
RT subclones.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, Brain, and Kidney;
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 FUNCTION, AND INTERACTION WITH TCP1 COMPLEX.
RX PubMed=16415341; DOI=10.1074/jbc.m513235200;
RA Stirling P.C., Cuellar J., Alfaro G.A., El Khadali F., Beh C.T.,
RA Valpuesta J.M., Melki R., Leroux M.R.;
RT "PhLP3 modulates CCT-mediated actin and tubulin folding via ternary
RT complexes with substrates.";
RL J. Biol. Chem. 281:7012-7021(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221 AND SER-223, AND
RP IDENTIFICATION BY 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).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Significantly diminishes the chaperonin TCP1 complex ATPase
CC activity, thus negatively impacts protein folding, including that of
CC actin or tubulin. {ECO:0000269|PubMed:16415341}.
CC -!- SUBUNIT: Forms ternary complexes with the chaperonin TCP1 complex,
CC spanning the cylindrical chaperonin cavity and contacting at least 2
CC subunits.
CC -!- INTERACTION:
CC O14530; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-707554, EBI-946029;
CC O14530; Q6ZUJ4: C3orf62; NbExp=3; IntAct=EBI-707554, EBI-2837036;
CC O14530; P0C7W6: CCDC172; NbExp=3; IntAct=EBI-707554, EBI-2548868;
CC O14530; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-707554, EBI-742887;
CC O14530; Q9H9E3: COG4; NbExp=5; IntAct=EBI-707554, EBI-368382;
CC O14530; Q8WWB3: DYDC1; NbExp=3; IntAct=EBI-707554, EBI-740680;
CC O14530; Q96B26: EXOSC8; NbExp=6; IntAct=EBI-707554, EBI-371922;
CC O14530; Q99689: FEZ1; NbExp=2; IntAct=EBI-707554, EBI-396435;
CC O14530; O14901: KLF11; NbExp=3; IntAct=EBI-707554, EBI-948266;
CC O14530; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-707554, EBI-1216080;
CC O14530; P43360: MAGEA6; NbExp=4; IntAct=EBI-707554, EBI-1045155;
CC O14530; Q15528-2: MED22; NbExp=3; IntAct=EBI-707554, EBI-12954271;
CC O14530; P52815: MRPL12; NbExp=3; IntAct=EBI-707554, EBI-358272;
CC O14530; P15173: MYOG; NbExp=4; IntAct=EBI-707554, EBI-3906629;
CC O14530; Q9BYU1: PBX4; NbExp=5; IntAct=EBI-707554, EBI-10302990;
CC O14530; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-707554, EBI-79165;
CC O14530; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-707554, EBI-302345;
CC O14530; Q8N6V9: TEX9; NbExp=3; IntAct=EBI-707554, EBI-746341;
CC O14530; P14373: TRIM27; NbExp=3; IntAct=EBI-707554, EBI-719493;
CC O14530; Q8N720: ZNF655; NbExp=3; IntAct=EBI-707554, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9CQ79}. Nucleus
CC {ECO:0000250|UniProtKB:Q9CQ79}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q9CQ79}. Midbody
CC {ECO:0000250|UniProtKB:Q9CQ79}. Note=Co-localizes with beta-tubulin in
CC the centrosome. {ECO:0000250|UniProtKB:Q9CQ79}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14530-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14530-2; Sequence=VSP_056553;
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DR EMBL; AB006679; BAA21881.1; -; mRNA.
DR EMBL; AK313777; BAG36515.1; -; mRNA.
DR EMBL; CR456935; CAG33216.1; -; mRNA.
DR EMBL; AK222616; BAD96336.1; -; mRNA.
DR EMBL; AB451403; BAG70217.1; -; mRNA.
DR EMBL; AC079447; AAX93257.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01869.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01870.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01871.1; -; Genomic_DNA.
DR EMBL; BC005968; AAH05968.1; -; mRNA.
DR EMBL; BC022864; AAH22864.1; -; mRNA.
DR EMBL; BC024223; AAH24223.2; -; mRNA.
DR EMBL; BC070183; AAH70183.2; -; mRNA.
DR CCDS; CCDS2044.1; -. [O14530-1]
DR RefSeq; NP_005774.2; NM_005783.3. [O14530-1]
DR AlphaFoldDB; O14530; -.
DR SMR; O14530; -.
DR BioGRID; 115487; 119.
DR IntAct; O14530; 68.
DR MINT; O14530; -.
DR STRING; 9606.ENSP00000264255; -.
DR GlyGen; O14530; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14530; -.
DR PhosphoSitePlus; O14530; -.
DR BioMuta; TXNDC9; -.
DR EPD; O14530; -.
DR jPOST; O14530; -.
DR MassIVE; O14530; -.
DR MaxQB; O14530; -.
DR PaxDb; O14530; -.
DR PeptideAtlas; O14530; -.
DR PRIDE; O14530; -.
DR ProteomicsDB; 48076; -. [O14530-1]
DR ProteomicsDB; 73969; -.
DR Antibodypedia; 32814; 144 antibodies from 27 providers.
DR DNASU; 10190; -.
DR Ensembl; ENST00000264255.8; ENSP00000264255.3; ENSG00000115514.12. [O14530-1]
DR Ensembl; ENST00000409434.5; ENSP00000387275.1; ENSG00000115514.12. [O14530-2]
DR GeneID; 10190; -.
DR KEGG; hsa:10190; -.
DR MANE-Select; ENST00000264255.8; ENSP00000264255.3; NM_005783.4; NP_005774.2.
DR UCSC; uc002szz.4; human. [O14530-1]
DR CTD; 10190; -.
DR DisGeNET; 10190; -.
DR GeneCards; TXNDC9; -.
DR HGNC; HGNC:24110; TXNDC9.
DR HPA; ENSG00000115514; Low tissue specificity.
DR MIM; 612564; gene.
DR neXtProt; NX_O14530; -.
DR OpenTargets; ENSG00000115514; -.
DR PharmGKB; PA134957934; -.
DR VEuPathDB; HostDB:ENSG00000115514; -.
DR eggNOG; KOG1672; Eukaryota.
DR GeneTree; ENSGT00390000015645; -.
DR HOGENOM; CLU_072378_2_0_1; -.
DR InParanoid; O14530; -.
DR OMA; QVLPCVI; -.
DR OrthoDB; 1444223at2759; -.
DR PhylomeDB; O14530; -.
DR TreeFam; TF313442; -.
DR PathwayCommons; O14530; -.
DR SignaLink; O14530; -.
DR BioGRID-ORCS; 10190; 36 hits in 1044 CRISPR screens.
DR ChiTaRS; TXNDC9; human.
DR GeneWiki; TXNDC9; -.
DR GenomeRNAi; 10190; -.
DR Pharos; O14530; Tbio.
DR PRO; PR:O14530; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O14530; protein.
DR Bgee; ENSG00000115514; Expressed in oocyte and 205 other tissues.
DR ExpressionAtlas; O14530; baseline and differential.
DR Genevisible; O14530; HS.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..226
FT /note="Thioredoxin domain-containing protein 9"
FT /id="PRO_0000120166"
FT DOMAIN 74..180
FT /note="Thioredoxin"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 188..226
FT /note="SGNLMEPPFQNQKKFGTNFTKLEKKTIRGKKYDSDSDDD -> R (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056553"
FT VARIANT 14
FT /note="L -> Q (in dbSNP:rs11542369)"
FT /id="VAR_058328"
FT VARIANT 38
FT /note="Q -> R (in dbSNP:rs11542371)"
FT /id="VAR_058329"
FT CONFLICT 122
FT /note="K -> N (in Ref. 1; BAA21881)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="N -> D (in Ref. 4; BAD96336)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="I -> M (in Ref. 1; BAA21881)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 26534 MW; 2735A2562D1143C3 CRC64;
MEADASVDMF SKVLEHQLLQ TTKLVEEHLD SEIQKLDQMD EDELERLKEK RLQALRKAQQ
QKQEWLSKGH GEYREIPSER DFFQEVKESE NVVCHFYRDS TFRCKILDRH LAILSKKHLE
TKFLKLNVEK APFLCERLHI KVIPTLALLK DGKTQDYVVG FTDLGNTDDF TTETLEWRLG
SSDILNYSGN LMEPPFQNQK KFGTNFTKLE KKTIRGKKYD SDSDDD
