TXD11_MOUSE
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 03-AUG-2022, entry version 143.
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 iPTMnet; Q8K2W3; -.
DR PhosphoSitePlus; Q8K2W3; -.
DR EPD; Q8K2W3; -.
DR MaxQB; Q8K2W3; -.
DR PaxDb; Q8K2W3; -.
DR PRIDE; Q8K2W3; -.
DR ProteomicsDB; 298440; -. [Q8K2W3-1]
DR ProteomicsDB; 298441; -. [Q8K2W3-2]
DR Antibodypedia; 49688; 124 antibodies from 25 providers.
DR DNASU; 106200; -.
DR Ensembl; ENSMUST00000038424; ENSMUSP00000041113; ENSMUSG00000022498. [Q8K2W3-1]
DR GeneID; 106200; -.
DR KEGG; mmu:106200; -.
DR UCSC; uc007yet.1; mouse. [Q8K2W3-1]
DR UCSC; uc007yew.1; mouse. [Q8K2W3-2]
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; 860125at2759; -.
DR PhylomeDB; Q8K2W3; -.
DR TreeFam; TF323602; -.
DR BioGRID-ORCS; 106200; 3 hits in 75 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 150 other tissues.
DR ExpressionAtlas; Q8K2W3; baseline and differential.
DR Genevisible; Q8K2W3; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
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
