TMX2_HUMAN
ID TMX2_HUMAN Reviewed; 296 AA.
AC Q9Y320; B7Z4R4; Q53G73; Q561W0; Q5J7Q7; Q8NBP9; Q9H3L1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Thioredoxin-related transmembrane protein 2;
DE AltName: Full=Cell proliferation-inducing gene 26 protein;
DE AltName: Full=Thioredoxin domain-containing protein 14;
DE Flags: Precursor;
GN Name=TMX2; Synonyms=TXNDC14;
GN ORFNames=CGI-31, My009, PIG26, PSEC0045, UNQ237/PRO270;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Mao Y.M., Xie Y., Zhou Z.X., Ying K., Zheng Z.H.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kim J.W.;
RT "Identification of a human proliferation inducing gene.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thyroid;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, and Eye;
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 TISSUE SPECIFICITY, MOTIF, AND DOMAIN.
RX PubMed=12670024; DOI=10.1023/a:1022073917044;
RA Meng X., Zhang C., Chen J., Peng S., Cao Y., Ying K., Xie Y., Mao Y.;
RT "Cloning and identification of a novel cDNA coding thioredoxin-related
RT transmembrane protein 2.";
RL Biochem. Genet. 41:99-106(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, 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 [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 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-211 AND SER-288, AND
RP IDENTIFICATION BY 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).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP INVOLVEMENT IN NEDMCMS, VARIANTS NEDMCMS CYS-53; ALA-55; ARG-56; HIS-62;
RP GLY-109; VAL-117; THR-178; GLN-205; TRP-231 AND 253-ARG--LYS-296 DEL,
RP CHARACTERIZATION OF VARIANTS NEDMCMS CYS-53; ALA-55; GLN-205; TRP-231 AND
RP 253-ARG--LYS-296 DEL, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION
RP WITH CANX AND ATP2A2, AND MUTAGENESIS OF CYS-170.
RX PubMed=31735293; DOI=10.1016/j.ajhg.2019.10.009;
RA Vandervore L.V., Schot R., Milanese C., Smits D.J., Kasteleijn E.,
RA Fry A.E., Pilz D.T., Brock S., Boerklue-Yuecel E., Post M.,
RA Bahi-Buisson N., Sanchez-Soler M.J., van Slegtenhorst M., Keren B.,
RA Afenjar A., Coury S.A., Tan W.H., Oegema R., de Vries L.S., Fawcett K.A.,
RA Nikkels P.G.J., Bertoli-Avella A., Al Hashem A., Alwabel A.A.,
RA Tlili-Graiess K., Efthymiou S., Zafar F., Rana N., Bibi F., Houlden H.,
RA Maroofian R., Person R.E., Crunk A., Savatt J.M., Turner L., Doosti M.,
RA Karimiani E.G., Saadi N.W., Akhondian J., Lequin M.H., Kayserili H.,
RA van der Spek P.J., Jansen A.C., Kros J.M., Verdijk R.M., Milosevic N.J.,
RA Fornerod M., Mastroberardino P.G., Mancini G.M.S.;
RT "TMX2 is a crucial regulator of cellular redox state, and its dysfunction
RT causes severe brain developmental abnormalities.";
RL Am. J. Hum. Genet. 105:1126-1147(2019).
RN [18]
RP STRUCTURE BY NMR OF 137-260.
RG RIKEN structural genomics initiative (RSGI);
RT "The solution structure of the thioredoxin domain of human thioredoxin-
RT related transmembrane protein 2.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [19]
RP VARIANT NEDMCMS GLN-205, AND CHARACTERIZATION OF VARIANT NEDMCMS GLN-205.
RX PubMed=31586943; DOI=10.1136/jmedgenet-2019-106409;
RA Ghosh S.G., Wang L., Breuss M.W., Green J.D., Stanley V., Yang X., Ross D.,
RA Traynor B.J., Alhashem A.M., Azam M., Selim L., Bastaki L.,
RA Elbastawisy H.I., Temtamy S., Zaki M., Gleeson J.G.;
RT "Recurrent homozygous damaging mutation in TMX2, encoding a protein
RT disulfide isomerase, in four families with microlissencephaly.";
RL J. Med. Genet. 57:274-282(2020).
CC -!- FUNCTION: Endoplasmic reticulum and mitochondria-associated protein
CC that probably functions as a regulator of cellular redox state and
CC thereby regulates protein post-translational modification, protein
CC folding and mitochondrial activity. Indirectly regulates neuronal
CC proliferation, migration, and organization in the developing brain.
CC {ECO:0000269|PubMed:31735293}.
CC -!- SUBUNIT: Monomer (PubMed:31735293). Homodimer; disulfide-linked
CC (PubMed:31735293). Occurs in both reduced and oxidized monomeric form
CC (PubMed:31735293). Oxidative conditions increase homodimerization
CC (PubMed:31735293). Interacts with CANX (PubMed:31735293). Interacts
CC with ATP2A2 (PubMed:31735293). {ECO:0000269|PubMed:31735293}.
CC -!- INTERACTION:
CC Q9Y320; Q9NRZ7: AGPAT3; NbExp=3; IntAct=EBI-6447886, EBI-2803601;
CC Q9Y320; Q9NRZ5: AGPAT4; NbExp=3; IntAct=EBI-6447886, EBI-1754287;
CC Q9Y320; Q9NUQ2: AGPAT5; NbExp=3; IntAct=EBI-6447886, EBI-6916385;
CC Q9Y320; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-6447886, EBI-11957045;
CC Q9Y320; Q13520: AQP6; NbExp=3; IntAct=EBI-6447886, EBI-13059134;
CC Q9Y320; Q9H2C2: ARV1; NbExp=3; IntAct=EBI-6447886, EBI-11724186;
CC Q9Y320; P07306: ASGR1; NbExp=3; IntAct=EBI-6447886, EBI-1172335;
CC Q9Y320; Q12797-6: ASPH; NbExp=3; IntAct=EBI-6447886, EBI-12092171;
CC Q9Y320; O15155: BET1; NbExp=3; IntAct=EBI-6447886, EBI-749204;
CC Q9Y320; Q12981: BNIP1; NbExp=3; IntAct=EBI-6447886, EBI-4402847;
CC Q9Y320; Q12982: BNIP2; NbExp=3; IntAct=EBI-6447886, EBI-752094;
CC Q9Y320; Q12983: BNIP3; NbExp=3; IntAct=EBI-6447886, EBI-749464;
CC Q9Y320; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-6447886, EBI-12244618;
CC Q9Y320; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-6447886, EBI-8648738;
CC Q9Y320; O14523: C2CD2L; NbExp=3; IntAct=EBI-6447886, EBI-12822627;
CC Q9Y320; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-6447886, EBI-9083477;
CC Q9Y320; P13500: CCL2; NbExp=3; IntAct=EBI-6447886, EBI-1034732;
CC Q9Y320; P60033: CD81; NbExp=3; IntAct=EBI-6447886, EBI-712921;
CC Q9Y320; O14735: CDIPT; NbExp=3; IntAct=EBI-6447886, EBI-358858;
CC Q9Y320; O95674: CDS2; NbExp=3; IntAct=EBI-6447886, EBI-3913685;
CC Q9Y320; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-6447886, EBI-2807956;
CC Q9Y320; Q4VAQ0: COL8A2; NbExp=3; IntAct=EBI-6447886, EBI-10241815;
CC Q9Y320; Q5RI15: COX20; NbExp=3; IntAct=EBI-6447886, EBI-2834035;
CC Q9Y320; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-6447886, EBI-12019274;
CC Q9Y320; Q5JRM2: CXorf66; NbExp=3; IntAct=EBI-6447886, EBI-12823659;
CC Q9Y320; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-6447886, EBI-2680384;
CC Q9Y320; P78329: CYP4F2; NbExp=3; IntAct=EBI-6447886, EBI-1752413;
CC Q9Y320; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-6447886, EBI-398977;
CC Q9Y320; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-6447886, EBI-12831978;
CC Q9Y320; P50402: EMD; NbExp=3; IntAct=EBI-6447886, EBI-489887;
CC Q9Y320; P54852: EMP3; NbExp=3; IntAct=EBI-6447886, EBI-3907816;
CC Q9Y320; Q7L5A8: FA2H; NbExp=3; IntAct=EBI-6447886, EBI-11337888;
CC Q9Y320; Q8N128-2: FAM177A1; NbExp=3; IntAct=EBI-6447886, EBI-12201693;
CC Q9Y320; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-6447886, EBI-12118888;
CC Q9Y320; Q92520: FAM3C; NbExp=3; IntAct=EBI-6447886, EBI-2876774;
CC Q9Y320; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-6447886, EBI-12142299;
CC Q9Y320; P37268: FDFT1; NbExp=3; IntAct=EBI-6447886, EBI-714550;
CC Q9Y320; Q9BWH2: FUNDC2; NbExp=3; IntAct=EBI-6447886, EBI-714482;
CC Q9Y320; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-6447886, EBI-11991950;
CC Q9Y320; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-6447886, EBI-6166686;
CC Q9Y320; P29033: GJB2; NbExp=3; IntAct=EBI-6447886, EBI-3905204;
CC Q9Y320; Q6Y1H2: HACD2; NbExp=3; IntAct=EBI-6447886, EBI-530257;
CC Q9Y320; Q9HCP6: HHATL; NbExp=3; IntAct=EBI-6447886, EBI-5916693;
CC Q9Y320; P30519: HMOX2; NbExp=3; IntAct=EBI-6447886, EBI-712096;
CC Q9Y320; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-6447886, EBI-1052304;
CC Q9Y320; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-6447886, EBI-18053395;
CC Q9Y320; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-6447886, EBI-3918847;
CC Q9Y320; Q9BUP3-3: HTATIP2; NbExp=3; IntAct=EBI-6447886, EBI-12937691;
CC Q9Y320; P46695: IER3; NbExp=3; IntAct=EBI-6447886, EBI-1748945;
CC Q9Y320; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-6447886, EBI-725665;
CC Q9Y320; P24593: IGFBP5; NbExp=3; IntAct=EBI-6447886, EBI-720480;
CC Q9Y320; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-6447886, EBI-8503746;
CC Q9Y320; P11215: ITGAM; NbExp=3; IntAct=EBI-6447886, EBI-2568251;
CC Q9Y320; O15243: LEPROT; NbExp=3; IntAct=EBI-6447886, EBI-15672507;
CC Q9Y320; O95214: LEPROTL1; NbExp=3; IntAct=EBI-6447886, EBI-750776;
CC Q9Y320; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-6447886, EBI-2820517;
CC Q9Y320; O95237: LRAT; NbExp=3; IntAct=EBI-6447886, EBI-13291307;
CC Q9Y320; Q13021: MALL; NbExp=3; IntAct=EBI-6447886, EBI-750078;
CC Q9Y320; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-6447886, EBI-11956541;
CC Q9Y320; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-6447886, EBI-373355;
CC Q9Y320; A0A0C4DFN3: MGLL; NbExp=3; IntAct=EBI-6447886, EBI-12866138;
CC Q9Y320; O14880: MGST3; NbExp=3; IntAct=EBI-6447886, EBI-724754;
CC Q9Y320; P30301: MIP; NbExp=3; IntAct=EBI-6447886, EBI-8449636;
CC Q9Y320; P12872: MLN; NbExp=3; IntAct=EBI-6447886, EBI-18053274;
CC Q9Y320; P11836: MS4A1; NbExp=3; IntAct=EBI-6447886, EBI-2808234;
CC Q9Y320; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-6447886, EBI-2863634;
CC Q9Y320; O95167: NDUFA3; NbExp=3; IntAct=EBI-6447886, EBI-1246131;
CC Q9Y320; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-6447886, EBI-10317425;
CC Q9Y320; Q8IXM6: NRM; NbExp=3; IntAct=EBI-6447886, EBI-10262547;
CC Q9Y320; Q15738: NSDHL; NbExp=3; IntAct=EBI-6447886, EBI-4280135;
CC Q9Y320; P42857: NSG1; NbExp=3; IntAct=EBI-6447886, EBI-6380741;
CC Q9Y320; Q53FV1: ORMDL2; NbExp=3; IntAct=EBI-6447886, EBI-11075081;
CC Q9Y320; Q9NUU6: OTULINL; NbExp=3; IntAct=EBI-6447886, EBI-6916492;
CC Q9Y320; P09466: PAEP; NbExp=3; IntAct=EBI-6447886, EBI-465167;
CC Q9Y320; I3L0A0: PEDS1-UBE2V1; NbExp=3; IntAct=EBI-6447886, EBI-12213001;
CC Q9Y320; Q9Y5Y5: PEX16; NbExp=3; IntAct=EBI-6447886, EBI-981985;
CC Q9Y320; Q99640-2: PKMYT1; NbExp=3; IntAct=EBI-6447886, EBI-12257782;
CC Q9Y320; Q04941: PLP2; NbExp=3; IntAct=EBI-6447886, EBI-608347;
CC Q9Y320; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-6447886, EBI-8652812;
CC Q9Y320; Q59EV6: PPGB; NbExp=3; IntAct=EBI-6447886, EBI-14210385;
CC Q9Y320; O60831: PRAF2; NbExp=3; IntAct=EBI-6447886, EBI-2506064;
CC Q9Y320; A5D903: PRB1; NbExp=3; IntAct=EBI-6447886, EBI-10173935;
CC Q9Y320; P43378: PTPN9; NbExp=3; IntAct=EBI-6447886, EBI-742898;
CC Q9Y320; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-6447886, EBI-712367;
CC Q9Y320; Q9BRK0: REEP2; NbExp=3; IntAct=EBI-6447886, EBI-11337973;
CC Q9Y320; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-6447886, EBI-7545592;
CC Q9Y320; Q96AA3: RFT1; NbExp=3; IntAct=EBI-6447886, EBI-6269616;
CC Q9Y320; Q9Y225-2: RNF24; NbExp=3; IntAct=EBI-6447886, EBI-13044680;
CC Q9Y320; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-6447886, EBI-10244780;
CC Q9Y320; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-6447886, EBI-8636004;
CC Q9Y320; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-6447886, EBI-3917235;
CC Q9Y320; Q8TAC9: SCAMP5; NbExp=3; IntAct=EBI-6447886, EBI-2695784;
CC Q9Y320; O00767: SCD; NbExp=3; IntAct=EBI-6447886, EBI-2684237;
CC Q9Y320; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-6447886, EBI-9679163;
CC Q9Y320; O75920: SERF1B; NbExp=3; IntAct=EBI-6447886, EBI-2115181;
CC Q9Y320; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-6447886, EBI-749270;
CC Q9Y320; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-6447886, EBI-2854842;
CC Q9Y320; Q9H9B4: SFXN1; NbExp=3; IntAct=EBI-6447886, EBI-355861;
CC Q9Y320; A0A1P0AYU5: SFXN3; NbExp=3; IntAct=EBI-6447886, EBI-14193895;
CC Q9Y320; Q96BI1: SLC22A18; NbExp=3; IntAct=EBI-6447886, EBI-11721845;
CC Q9Y320; P78382: SLC35A1; NbExp=3; IntAct=EBI-6447886, EBI-12870360;
CC Q9Y320; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-6447886, EBI-10226799;
CC Q9Y320; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-6447886, EBI-8640191;
CC Q9Y320; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-6447886, EBI-12188413;
CC Q9Y320; P02808: STATH; NbExp=3; IntAct=EBI-6447886, EBI-738687;
CC Q9Y320; Q86Y82: STX12; NbExp=3; IntAct=EBI-6447886, EBI-2691717;
CC Q9Y320; Q13277: STX3; NbExp=3; IntAct=EBI-6447886, EBI-1394295;
CC Q9Y320; O15400: STX7; NbExp=3; IntAct=EBI-6447886, EBI-3221827;
CC Q9Y320; P07204: THBD; NbExp=3; IntAct=EBI-6447886, EBI-941422;
CC Q9Y320; C9JKN6: THSD7B; NbExp=3; IntAct=EBI-6447886, EBI-17192156;
CC Q9Y320; P55061: TMBIM6; NbExp=3; IntAct=EBI-6447886, EBI-1045825;
CC Q9Y320; Q12893: TMEM115; NbExp=3; IntAct=EBI-6447886, EBI-8633987;
CC Q9Y320; Q9BXJ8: TMEM120A; NbExp=3; IntAct=EBI-6447886, EBI-727322;
CC Q9Y320; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-6447886, EBI-10171534;
CC Q9Y320; Q9BTD3: TMEM121; NbExp=3; IntAct=EBI-6447886, EBI-12155101;
CC Q9Y320; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-6447886, EBI-10694905;
CC Q9Y320; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-6447886, EBI-2844246;
CC Q9Y320; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-6447886, EBI-8638294;
CC Q9Y320; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-6447886, EBI-2339195;
CC Q9Y320; Q96HP8: TMEM176A; NbExp=3; IntAct=EBI-6447886, EBI-2800645;
CC Q9Y320; Q5SNT2-2: TMEM201; NbExp=3; IntAct=EBI-6447886, EBI-11994282;
CC Q9Y320; Q969S6: TMEM203; NbExp=3; IntAct=EBI-6447886, EBI-12274070;
CC Q9Y320; Q9BTX3: TMEM208; NbExp=3; IntAct=EBI-6447886, EBI-12876824;
CC Q9Y320; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-6447886, EBI-347385;
CC Q9Y320; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-6447886, EBI-11528917;
CC Q9Y320; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-6447886, EBI-11956809;
CC Q9Y320; P56557: TMEM50B; NbExp=3; IntAct=EBI-6447886, EBI-12366453;
CC Q9Y320; Q9NW97: TMEM51; NbExp=3; IntAct=EBI-6447886, EBI-726044;
CC Q9Y320; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-6447886, EBI-6656213;
CC Q9Y320; Q6P5X7-2: TMEM71; NbExp=5; IntAct=EBI-6447886, EBI-12886878;
CC Q9Y320; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-6447886, EBI-2548832;
CC Q9Y320; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-6447886, EBI-12111910;
CC Q9Y320; Q9Y320: TMX2; NbExp=3; IntAct=EBI-6447886, EBI-6447886;
CC Q9Y320; Q6ZUI0: TPRG1; NbExp=3; IntAct=EBI-6447886, EBI-17249488;
CC Q9Y320; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-6447886, EBI-11996766;
CC Q9Y320; Q9NSU2-1: TREX1; NbExp=3; IntAct=EBI-6447886, EBI-16746122;
CC Q9Y320; A0AVG3: TSNARE1; NbExp=3; IntAct=EBI-6447886, EBI-12003468;
CC Q9Y320; O60636: TSPAN2; NbExp=3; IntAct=EBI-6447886, EBI-3914288;
CC Q9Y320; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-6447886, EBI-10243654;
CC Q9Y320; Q9NYZ1: TVP23B; NbExp=3; IntAct=EBI-6447886, EBI-11343401;
CC Q9Y320; Q9Y385: UBE2J1; NbExp=3; IntAct=EBI-6447886, EBI-988826;
CC Q9Y320; Q86WB7-2: UNC93A; NbExp=3; IntAct=EBI-6447886, EBI-13356252;
CC Q9Y320; P23763-3: VAMP1; NbExp=3; IntAct=EBI-6447886, EBI-12097582;
CC Q9Y320; Q15836: VAMP3; NbExp=3; IntAct=EBI-6447886, EBI-722343;
CC Q9Y320; O75379: VAMP4; NbExp=3; IntAct=EBI-6447886, EBI-744953;
CC Q9Y320; O95183: VAMP5; NbExp=3; IntAct=EBI-6447886, EBI-10191195;
CC Q9Y320; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-6447886, EBI-1059156;
CC Q9Y320; O95292: VAPB; NbExp=3; IntAct=EBI-6447886, EBI-1188298;
CC Q9Y320; Q14508: WFDC2; NbExp=3; IntAct=EBI-6447886, EBI-723529;
CC Q9Y320; O95070: YIF1A; NbExp=3; IntAct=EBI-6447886, EBI-2799703;
CC Q9Y320; Q9Y548: YIPF1; NbExp=3; IntAct=EBI-6447886, EBI-7850136;
CC Q9Y320; Q9BWQ6: YIPF2; NbExp=3; IntAct=EBI-6447886, EBI-751204;
CC Q9Y320; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-6447886, EBI-751210;
CC Q9Y320; Q96FB2; NbExp=3; IntAct=EBI-6447886, EBI-2857623;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:31735293}; Single-pass type I membrane protein
CC {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:31735293}.
CC Note=Localizes to endoplasmic reticulum mitochondria-associated
CC membrane (MAMs) that connect the endoplasmic reticulum and the
CC mitochondria. {ECO:0000269|PubMed:31735293}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y320-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y320-2; Sequence=VSP_030696;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12670024}.
CC -!- DOMAIN: The thioredoxin domain lacks the 2 redox-active cysteines,
CC suggesting that it lacks thioredoxin activity. {ECO:0000305}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000305|PubMed:12670024}.
CC -!- DISEASE: Neurodevelopmental disorder with microcephaly, cortical
CC malformations, and spasticity (NEDMCMS) [MIM:618730]: An autosomal
CC recessive neurodevelopmental disorder characterized by developmental
CC delay, severe to profound intellectual disability, congenital
CC microcephaly, cortical polymicrogyria, lissencephaly, reduced central
CC white matter volume, and drug-resistant epilepsy, lack of speech,
CC absent ambulation and a progressive neurodegenerative course in most
CC patients. Early death may occur in some patients.
CC {ECO:0000269|PubMed:31586943, ECO:0000269|PubMed:31735293}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG43122.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC11569.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF132965; AAD27740.1; -; mRNA.
DR EMBL; AY358501; AAQ88865.1; -; mRNA.
DR EMBL; AK297688; BAH12650.1; -; mRNA.
DR EMBL; AK075359; BAC11569.1; ALT_FRAME; mRNA.
DR EMBL; AF059753; AAG43122.1; ALT_FRAME; mRNA.
DR EMBL; AY451237; AAS66642.1; -; mRNA.
DR EMBL; AK223058; BAD96778.1; -; mRNA.
DR EMBL; BC000666; AAH00666.1; -; mRNA.
DR EMBL; BC093062; AAH93062.1; -; mRNA.
DR CCDS; CCDS44601.1; -. [Q9Y320-2]
DR CCDS; CCDS7967.1; -. [Q9Y320-1]
DR RefSeq; NP_001137484.1; NM_001144012.2. [Q9Y320-2]
DR RefSeq; NP_057043.1; NM_015959.3. [Q9Y320-1]
DR PDB; 2DJ0; NMR; -; A=137-260.
DR PDBsum; 2DJ0; -.
DR AlphaFoldDB; Q9Y320; -.
DR BMRB; Q9Y320; -.
DR SMR; Q9Y320; -.
DR BioGRID; 119266; 245.
DR IntAct; Q9Y320; 179.
DR MINT; Q9Y320; -.
DR STRING; 9606.ENSP00000278422; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q9Y320; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y320; -.
DR PhosphoSitePlus; Q9Y320; -.
DR SwissPalm; Q9Y320; -.
DR BioMuta; TMX2; -.
DR DMDM; 74735249; -.
DR EPD; Q9Y320; -.
DR jPOST; Q9Y320; -.
DR MassIVE; Q9Y320; -.
DR MaxQB; Q9Y320; -.
DR PaxDb; Q9Y320; -.
DR PeptideAtlas; Q9Y320; -.
DR PRIDE; Q9Y320; -.
DR ProteomicsDB; 85962; -. [Q9Y320-1]
DR ProteomicsDB; 85963; -. [Q9Y320-2]
DR Antibodypedia; 27473; 96 antibodies from 21 providers.
DR DNASU; 51075; -.
DR Ensembl; ENST00000278422.9; ENSP00000278422.4; ENSG00000213593.10. [Q9Y320-1]
DR Ensembl; ENST00000378312.8; ENSP00000367562.4; ENSG00000213593.10. [Q9Y320-2]
DR GeneID; 51075; -.
DR KEGG; hsa:51075; -.
DR MANE-Select; ENST00000278422.9; ENSP00000278422.4; NM_015959.4; NP_057043.1.
DR UCSC; uc001nlc.3; human. [Q9Y320-1]
DR CTD; 51075; -.
DR DisGeNET; 51075; -.
DR GeneCards; TMX2; -.
DR HGNC; HGNC:30739; TMX2.
DR HPA; ENSG00000213593; Low tissue specificity.
DR MalaCards; TMX2; -.
DR MIM; 616715; gene.
DR MIM; 618730; phenotype.
DR neXtProt; NX_Q9Y320; -.
DR OpenTargets; ENSG00000213593; -.
DR PharmGKB; PA164726611; -.
DR VEuPathDB; HostDB:ENSG00000213593; -.
DR eggNOG; KOG0914; Eukaryota.
DR GeneTree; ENSGT00390000003751; -.
DR HOGENOM; CLU_064868_0_0_1; -.
DR InParanoid; Q9Y320; -.
DR OMA; FYTAWNP; -.
DR OrthoDB; 1107509at2759; -.
DR PhylomeDB; Q9Y320; -.
DR TreeFam; TF314606; -.
DR PathwayCommons; Q9Y320; -.
DR SignaLink; Q9Y320; -.
DR BioGRID-ORCS; 51075; 341 hits in 1095 CRISPR screens.
DR EvolutionaryTrace; Q9Y320; -.
DR GenomeRNAi; 51075; -.
DR Pharos; Q9Y320; Tbio.
DR PRO; PR:Q9Y320; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y320; protein.
DR Bgee; ENSG00000213593; Expressed in mucosa of transverse colon and 198 other tissues.
DR ExpressionAtlas; Q9Y320; baseline and differential.
DR Genevisible; Q9Y320; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043227; C:membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IMP:UniProtKB.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR CDD; cd02962; TMX2; 1.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR039101; TMX2.
DR InterPro; IPR037463; TMX2_thioredoxin_dom.
DR PANTHER; PTHR15853; PTHR15853; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Disulfide bond;
KW Endoplasmic reticulum; Intellectual disability; Lissencephaly; Membrane;
KW Mitochondrion; Neurodegeneration; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..48
FT /evidence="ECO:0000255"
FT CHAIN 49..296
FT /note="Thioredoxin-related transmembrane protein 2"
FT /id="PRO_0000315752"
FT TOPO_DOM 49..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 114..269
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 269..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 293..296
FT /note="Di-lysine motif"
FT /evidence="ECO:0000305|PubMed:12670024"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 84..122
FT /note="ITVEQHIGNIFMFSKVANTILFFRLDIRMGLLYITLCIV -> M (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030696"
FT VARIANT 53
FT /note="R -> C (in NEDMCMS; increased homodimerization; even
FT in absence of oxidative stress; dbSNP:rs145634348)"
FT /evidence="ECO:0000269|PubMed:31735293"
FT /id="VAR_083593"
FT VARIANT 55
FT /note="D -> A (in NEDMCMS; unknown pathological
FT significance; dbSNP:rs1398376742)"
FT /evidence="ECO:0000269|PubMed:31735293"
FT /id="VAR_083594"
FT VARIANT 56
FT /note="G -> R (in NEDMCMS; unknown pathological
FT significance; dbSNP:rs367990143)"
FT /evidence="ECO:0000269|PubMed:31735293"
FT /id="VAR_083595"
FT VARIANT 62
FT /note="D -> H (in NEDMCMS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31735293"
FT /id="VAR_083596"
FT VARIANT 109
FT /note="D -> G (in NEDMCMS; unknown pathological
FT significance; dbSNP:rs750470937)"
FT /evidence="ECO:0000269|PubMed:31735293"
FT /id="VAR_083597"
FT VARIANT 117
FT /note="I -> V (in NEDMCMS; unknown pathological
FT significance; dbSNP:rs748116606)"
FT /evidence="ECO:0000269|PubMed:31735293"
FT /id="VAR_083598"
FT VARIANT 178
FT /note="A -> T (in NEDMCMS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31735293"
FT /id="VAR_083599"
FT VARIANT 205
FT /note="R -> Q (in NEDMCMS; changed alternative splicing;
FT decreased protein abundance; homozygous patient cells show
FT decreased mitochondrial respiratory reserve capacity and
FT compensatory increased glycolytic activity;
FT dbSNP:rs370455806)"
FT /evidence="ECO:0000305|PubMed:31586943,
FT ECO:0000305|PubMed:31735293"
FT /id="VAR_083600"
FT VARIANT 231
FT /note="R -> W (in NEDMCMS; increased homodimerization; even
FT in absence of oxidative stress; dbSNP:rs759161110)"
FT /evidence="ECO:0000269|PubMed:31735293"
FT /id="VAR_083601"
FT VARIANT 253..296
FT /note="Missing (in NEDMCMS)"
FT /evidence="ECO:0000269|PubMed:31735293"
FT /id="VAR_083602"
FT MUTAGEN 170
FT /note="C->G: Increased homodimerization even in absence of
FT oxidative stress."
FT /evidence="ECO:0000269|PubMed:31735293"
FT CONFLICT 90
FT /note="I -> T (in Ref. 6; AAS66642)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="I -> V (in Ref. 6; AAS66642)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="D -> S (in Ref. 5; AAG43122)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="N -> S (in Ref. 7; BAD96778)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="D -> E (in Ref. 7; BAD96778)"
FT /evidence="ECO:0000305"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:2DJ0"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:2DJ0"
FT TURN 169..173
FT /evidence="ECO:0007829|PDB:2DJ0"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:2DJ0"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2DJ0"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:2DJ0"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:2DJ0"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:2DJ0"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:2DJ0"
FT STRAND 217..233
FT /evidence="ECO:0007829|PDB:2DJ0"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:2DJ0"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:2DJ0"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:2DJ0"
SQ SEQUENCE 296 AA; 34038 MW; D646B16B3A5F0C6D CRC64;
MAVLAPLIAL VYSVPRLSRW LAQPYYLLSA LLSAAFLLVR KLPPLCHGLP TQREDGNPCD
FDWREVEILM FLSAIVMMKN RRSITVEQHI GNIFMFSKVA NTILFFRLDI RMGLLYITLC
IVFLMTCKPP LYMGPEYIKY FNDKTIDEEL ERDKRVTWIV EFFANWSNDC QSFAPIYADL
SLKYNCTGLN FGKVDVGRYT DVSTRYKVST SPLTKQLPTL ILFQGGKEAM RRPQIDKKGR
AVSWTFSEEN VIREFNLNEL YQRAKKLSKA GDNIPEEQPV ASTPTTVSDG ENKKDK
