ID   TXD11_BOVIN             Reviewed;         957 AA.
AC   A4FUW8;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Thioredoxin domain-containing protein 11;
GN   Name=TXNDC11;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; BC123384; AAI23385.1; -; mRNA.
DR   RefSeq; NP_001076889.1; NM_001083420.1.
DR   AlphaFoldDB; A4FUW8; -.
DR   SMR; A4FUW8; -.
DR   STRING; 9913.ENSBTAP00000019741; -.
DR   PaxDb; A4FUW8; -.
DR   GeneID; 513509; -.
DR   KEGG; bta:513509; -.
DR   CTD; 51061; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   InParanoid; A4FUW8; -.
DR   OrthoDB; 860125at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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   2: Evidence at transcript level;
KW   Coiled coil; Disulfide bond; Endoplasmic reticulum; Membrane;
KW   Redox-active center; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..957
FT                   /note="Thioredoxin domain-containing protein 11"
FT                   /id="PRO_0000297489"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          91..213
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          621..771
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          904..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          785..889
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        904..920
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        937..957
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        441..444
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        691..694
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   957 AA;  107366 MW;  714582E18B6CB6D3 CRC64;
     MSECGGRGGG GGSSSSSDDA EDEGGGGGPA GSGSLSPAPA ASSEGRLRRG LRGASLMARR
     RPELLCGAVA LGCALLLALK FTCSRAKDVI IPAKPPVSFF SSRSPVLDLF QGQLDYAEHI
     RRDSEVVLLF FYAPWCGQSI AARAEIEQAA SRLSDQVLFV AINCWWNQGK CRKQKHFFYF
     PVIYLYHRSF GPIEYKGPMS AVYIEKFVRR VMKPLLYIPS QSELLDFLSN YEPGVLGYFE
     FSGSPQPPGY LTFFTSALHS LKKDYLGTVR FGVITNKHLA KLVSLVHSGS VYLHRHFNTS
     LVFPREVINY TAENICKWAL ENRETLVRWL WPHGGKSLLL NNELKKGPAL FVFIPFNPLA
     ESHPLIDEIT EVALEYNNCH GDQVVERLLQ HLRRVDAPAF KSLAPDPPAR LPDPPLITAS
     PCCNTVVLPR WHSISRTHNV CELCVNQTAG GLRPSSVSMP QCSFFEMAAA LDSFYLKEQT
     FYHVVSDSIE CSNFLSFYSP FSYYTACCRT INRGVAGFID SEQGVFETPP VAFSSLEKKC
     EVESPGSVPH IEENRYLFPE LETSSSSFTG LSCRTNKTLN IYLLDSNLFW LYAERLGAPS
     AARVKEFATI VDVKEESHYI LDPKQALMKF TLESFIQNFS VLYSPLKRHL IGSDSTQFTS
     QRLITEVTTD TFWEVVLQKQ DVLLLYYAQW CGFCPALNHV FIQLARLLPS DTFTVARIDV
     SQNDLPWEFM VDRLPTVLFF PCNRKDLSVK YPEDLPITLP NLLRFILHHS DPASDPRNLA
     GPPTAECLQN EAVLQQGHIA HLEREIRKLR AEIGTLQRAQ VQVEARLASA RRDEHRLLRQ
     QHTLERQHDL LRLHSEQLQA LYEHKTRELD EVARKLQELA DASETLLTEN TWLKILVATM
     EQRLEGRDGA DDRVPPSKAR SEHPEPPGAP RLPASTPLPA NISSTLASEG SPENRTD