ID   TXD16_MOUSE             Reviewed;         820 AA.
AC   Q7TN22; Q69ZL5; Q8BL40; Q8R2W8; Q9CS82;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Thioredoxin domain-containing protein 16;
DE   Flags: Precursor;
GN   Name=Txndc16 {ECO:0000312|MGI:MGI:1917811}; Synonyms=Kiaa1344;
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 1).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-354.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary gland;
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).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9P2K2}.
CC       Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q9P2K2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TN22-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TN22-2; Sequence=VSP_021364;
CC   -!- DOMAIN: Contains a masked and non-functional KDEL endoplasmic reticulum
CC       retrieval motif. {ECO:0000250|UniProtKB:Q9P2K2}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9P2K2}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32431.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK173153; BAD32431.1; ALT_INIT; mRNA.
DR   EMBL; AK017582; BAB30819.1; -; mRNA.
DR   EMBL; AK046466; BAC32743.1; -; mRNA.
DR   EMBL; BC027108; AAH27108.1; -; mRNA.
DR   EMBL; BC052488; AAH52488.1; -; mRNA.
DR   CCDS; CCDS26973.1; -. [Q7TN22-2]
DR   CCDS; CCDS79300.1; -. [Q7TN22-1]
DR   RefSeq; NP_001297463.1; NM_001310534.1. [Q7TN22-1]
DR   RefSeq; NP_766185.1; NM_172597.3. [Q7TN22-2]
DR   RefSeq; XP_006519583.1; XM_006519520.3. [Q7TN22-1]
DR   RefSeq; XP_011243482.1; XM_011245180.2. [Q7TN22-1]
DR   RefSeq; XP_017171675.1; XM_017316186.1. [Q7TN22-1]
DR   AlphaFoldDB; Q7TN22; -.
DR   SMR; Q7TN22; -.
DR   STRING; 10090.ENSMUSP00000022377; -.
DR   GlyGen; Q7TN22; 1 site.
DR   iPTMnet; Q7TN22; -.
DR   PhosphoSitePlus; Q7TN22; -.
DR   EPD; Q7TN22; -.
DR   MaxQB; Q7TN22; -.
DR   PaxDb; Q7TN22; -.
DR   PeptideAtlas; Q7TN22; -.
DR   PRIDE; Q7TN22; -.
DR   ProteomicsDB; 298393; -. [Q7TN22-1]
DR   ProteomicsDB; 298394; -. [Q7TN22-2]
DR   Antibodypedia; 149; 36 antibodies from 16 providers.
DR   DNASU; 70561; -.
DR   Ensembl; ENSMUST00000022377; ENSMUSP00000022377; ENSMUSG00000021830. [Q7TN22-2]
DR   Ensembl; ENSMUST00000123879; ENSMUSP00000123023; ENSMUSG00000021830. [Q7TN22-1]
DR   Ensembl; ENSMUST00000139526; ENSMUSP00000120287; ENSMUSG00000021830. [Q7TN22-1]
DR   GeneID; 70561; -.
DR   KEGG; mmu:70561; -.
DR   UCSC; uc007tge.1; mouse. [Q7TN22-2]
DR   UCSC; uc007tgf.1; mouse. [Q7TN22-1]
DR   CTD; 57544; -.
DR   MGI; MGI:1917811; Txndc16.
DR   VEuPathDB; HostDB:ENSMUSG00000021830; -.
DR   eggNOG; KOG0191; Eukaryota.
DR   GeneTree; ENSGT00390000006080; -.
DR   HOGENOM; CLU_018100_1_0_1; -.
DR   InParanoid; Q7TN22; -.
DR   OMA; HANVVFK; -.
DR   OrthoDB; 1124691at2759; -.
DR   PhylomeDB; Q7TN22; -.
DR   TreeFam; TF328825; -.
DR   BioGRID-ORCS; 70561; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Txndc16; mouse.
DR   PRO; PR:Q7TN22; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q7TN22; protein.
DR   Bgee; ENSMUSG00000021830; Expressed in animal zygote and 243 other tissues.
DR   ExpressionAtlas; Q7TN22; baseline and differential.
DR   Genevisible; Q7TN22; MM.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR040090; TXNDC16.
DR   PANTHER; PTHR22699; PTHR22699; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..820
FT                   /note="Thioredoxin domain-containing protein 16"
FT                   /id="PRO_0000257790"
FT   DOMAIN          394..496
FT                   /note="Thioredoxin"
FT   MOTIF           817..820
FT                   /note="Mediates endoplasmic reticulum retention"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2K2"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        450..457
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2K2"
FT   VAR_SEQ         733..734
FT                   /note="TV -> I (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_021364"
SQ   SEQUENCE   820 AA;  92105 MW;  6006949E004D2BC0 CRC64;
     MMSSGFSVFR AGVALVLMCS FYKSTEDSLP ELTPQQYFST LQPGKASLVY FCQVGSLSNS
     VFLEELKEAV KPLQDYGISV AKVTCVEEEA SRYCGEEEGL MKAYLFRGNI LLREFPTDIL
     FDVNAIIAHV LFALLFNEVK YITTLEDLHS IENSLKGKSN MIFSYVEAIG TPEHRAVMEA
     AFVYGTSYQF ALTTEIALLE NIGSESIEHA HLYFFHCKLV LDLTEHCRRT LMEQPLTTLN
     IHVFVKTMNA PLLMEVAEDP QQVSTVHLQL GLPLVFIISQ RATQEADRRT AEWVAWHLLG
     KAGVLLLLRD SMDVNIPQHA NVAFRRAEKD VPVEFLVLND VELIISHVKN NMHIEEIQED
     EGEDMEGPDL AVEDDEVAGT VYRDRKKPLP LELSVELTEE TFNTTVMTSD SIVLFYATWH
     AVSMAFLQSY IDVAIKLKGR STILLTRINC ADWSDICTKQ NVTAFPVVKL YKEGESPVSY
     AGMLATKDLL KFIQLNKISC PVNIASIQEA EKYLRGELYK DLPSSASVSV LGLFSPAMAS
     AKELFREAGK QLRGSVITGI YSEDDVWILS NKYATTLPAL LLARPKEGRI ESVPLDTTLV
     QDMAQILANA LLEAFPEITV ENLPTYLRFQ RPLLLLFSGG SINPQYRNTI LALVRQKQLD
     SFTPCWLNLK NTPVGRGILK AYFGRLPPLP QLLLVNLHSG GQVYAFPSSQ SVTEQSLVLW
     LKHLQAGLEN PITVLSAQEW KPPLPAFDFL NMMDAPTSQA PTKKVLECQK EAEVQESAEL
     QPGDRSTARR EPVEMLRIKR WNTANWPKDT QEPFHHDKEL