ID   TXD11_MOUSE             Reviewed;         948 AA.
AC   Q8K2W3; Q8BMR8; Q8VCK9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 151.
DE   RecName: Full=Thioredoxin domain-containing protein 11;
GN   Name=Txndc11;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Skin;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, and 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).
CC   -!- FUNCTION: May act as a redox regulator involved in DUOX proteins
CC       folding. The interaction with DUOX1 and DUOX2 suggest that it belongs
CC       to a multiprotein complex constituting the thyroid H(2)O(2) generating
CC       system. It is however not sufficient to assist DUOX1 and DUOX2 in
CC       H(2)O(2) generation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the cytoplasmic part of DUOX1 and DUOX2.
CC       Interacts with TPO and CYBA (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K2W3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K2W3-2; Sequence=VSP_014338, VSP_014339;
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH19564.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK029166; BAC26333.1; -; mRNA.
DR   EMBL; BC019564; AAH19564.1; ALT_INIT; mRNA.
DR   EMBL; BC029643; AAH29643.1; -; mRNA.
DR   CCDS; CCDS27960.1; -. [Q8K2W3-1]
DR   RefSeq; NP_083858.1; NM_029582.2. [Q8K2W3-1]
DR   RefSeq; NP_598866.1; NM_134105.2.
DR   AlphaFoldDB; Q8K2W3; -.
DR   SMR; Q8K2W3; -.
DR   STRING; 10090.ENSMUSP00000041113; -.
DR   GlyGen; Q8K2W3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8K2W3; -.
DR   PhosphoSitePlus; Q8K2W3; -.
DR   EPD; Q8K2W3; -.
DR   MaxQB; Q8K2W3; -.
DR   PaxDb; 10090-ENSMUSP00000041113; -.
DR   ProteomicsDB; 298440; -. [Q8K2W3-1]
DR   ProteomicsDB; 298441; -. [Q8K2W3-2]
DR   Antibodypedia; 49688; 144 antibodies from 25 providers.
DR   DNASU; 106200; -.
DR   Ensembl; ENSMUST00000038424.14; ENSMUSP00000041113.8; ENSMUSG00000022498.17. [Q8K2W3-1]
DR   GeneID; 106200; -.
DR   KEGG; mmu:106200; -.
DR   UCSC; uc007yet.1; mouse. [Q8K2W3-1]
DR   UCSC; uc007yew.1; mouse. [Q8K2W3-2]
DR   AGR; MGI:1923620; -.
DR   CTD; 51061; -.
DR   MGI; MGI:1923620; Txndc11.
DR   VEuPathDB; HostDB:ENSMUSG00000022498; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   GeneTree; ENSGT00390000016020; -.
DR   InParanoid; Q8K2W3; -.
DR   OMA; ANDLPWE; -.
DR   OrthoDB; 4541374at2759; -.
DR   PhylomeDB; Q8K2W3; -.
DR   TreeFam; TF323602; -.
DR   BioGRID-ORCS; 106200; 3 hits in 80 CRISPR screens.
DR   ChiTaRS; Txndc11; mouse.
DR   PRO; PR:Q8K2W3; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q8K2W3; Protein.
DR   Bgee; ENSMUSG00000022498; Expressed in ectoplacental cone and 153 other cell types or tissues.
DR   ExpressionAtlas; Q8K2W3; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd03006; PDI_a_EFP1_N; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd02981; PDI_b_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR46497; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 11; 1.
DR   PANTHER; PTHR46497:SF1; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 11; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
DR   Genevisible; Q8K2W3; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Disulfide bond; Endoplasmic reticulum;
KW   Membrane; Phosphoprotein; Redox-active center; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..948
FT                   /note="Thioredoxin domain-containing protein 11"
FT                   /id="PRO_0000120174"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          88..214
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          618..768
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..948
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          793..874
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        914..940
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         798
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PKC3"
FT   DISULFID        438..441
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        688..691
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   VAR_SEQ         230..236
FT                   /note="PGVLGYF -> KQQATQY (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014338"
FT   VAR_SEQ         237..948
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014339"
SQ   SEQUENCE   948 AA;  105959 MW;  23AAC6C544919DC1 CRC64;
     MSECGGRGGG GGNNSEDAED EGGGPKGSGS LSPAGAAASL EGRIRRGLRG ASLMARQRPE
     LLCGAVALGC ALLFALKFTC SRAKDVIIPA KPPVSFFSSR SPVLDLFQGQ LDYADHVRQD
     SEVVVLFFYA PWCGQSIAAR AEIEQAASRL SDQVLFVAIN CWWNQGKCRK QKHFFYFPVI
     HLYHRSFGPI EYKGPMSAVY IEKFVRRAMK PLLYIPSQSA LLDFLSSYEP GVLGYFEFSG
     SPQPPGYLTF FTSALHSLKK DYLGTVRFGV ITDKHLARLV SLVHSGSVYL HRHFNTSLVF
     PREVMNFTAE NIYKWASENQ ETLFRWLQPH GGKSLLLNNE LKKGPALFLF IPFDPLAERH
     PLLDEITEVA LEYNNCHGDQ VVERLLQHLR RVEAPVLQSL APELPASLPD TQLMAASPCC
     NTVVLPQGPA LSRTHNVCEL CVNQTVGGTR PSSVSVPQCS FFEMAAALDS FYLKEQTFYH
     VVSGSIECSN FLTSYSPFSY YTACCRTISR GMASFTGSEQ NVLTAPAIEF SSLEKSCEAT
     APSSIPHIEE NRYRFPQVGL TSTAFTGLSC RTNKTLNIYL LDSNLFWLYA ERLGAPSSAP
     VKEFATIVDV KEESHYILDP KQALMKFTLE SFIQNFSVLY SPLKRHLTGS DSAQFPTQHL
     ITEVTTDTFW EVTLRKQDVL LLYYTQWCGF CPSLNHIFIQ LARLLPEDTF TVARIDVSQN
     DLPWEFMVDR LPTVLFFPCN RKDLSVKYPG DLPITLPNLL RFILHHSDAA SAPQDPGISP
     PTQDCVQSKA VLQREHISHV ENAMQKLRSE MSSLRRTQEQ VEGRLLSARR DGHRLLRRQR
     TLEQQHRLLR RHSQKLQALY LKKARELQEL ARASGTPLPE HTWLKILVAT MERELEGQGG
     AKEPAPLGKA RPNHSKSMGT TQLPGDTPPP STTSSTLASE TKHENRTD
//