ID TXD16_HUMAN Reviewed; 825 AA. AC Q9P2K2; A5PKW9; A7E260; A7MD07; B9EH67; Q9H9W7; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 4. DT 10-JUN-2026, entry version 165. DE RecName: Full=Thioredoxin domain-containing protein 16 {ECO:0000312|HGNC:HGNC:19965}; DE Flags: Precursor; GN Name=TXNDC16 {ECO:0000312|HGNC:HGNC:19965}; GN Synonyms=ERP90 {ECO:0000303|PubMed:21359175}, KIAA1344; 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], AND VARIANT LYS-486. RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [2] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-486. RC TISSUE=Lung, and Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 456-825. 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 [6] RP SUBCELLULAR LOCATION, INTERACTION WITH FOXRED2, DISULFIDE BONDS, AND RP GLYCOSYLATION. RX PubMed=21359175; DOI=10.1371/journal.pone.0017037; RA Riemer J., Hansen H.G., Appenzeller-Herzog C., Johansson L., Ellgaard L.; RT "Identification of the PDI-family member ERp90 as an interaction partner of RT ERFAD."; RL PLoS ONE 6:E17037-E17037(2011). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=25122923; DOI=10.4049/jimmunol.1303098; RA Harz C., Ludwig N., Lang S., Werner T.V., Galata V., Backes C., Schmitt K., RA Nickels R., Krause E., Jung M., Rettig J., Keller A., Menger M., RA Zimmermann R., Meese E.; RT "Secretion and immunogenicity of the meningioma-associated antigen RT TXNDC16."; RL J. Immunol. 193:3146-3154(2014). CC -!- SUBUNIT: Interacts with FOXRED2. {ECO:0000269|PubMed:21359175}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25122923}. CC Endoplasmic reticulum lumen {ECO:0000269|PubMed:21359175, CC ECO:0000269|PubMed:25122923}. CC -!- DOMAIN: Contains a masked and non-functional KDEL endoplasmic reticulum CC retrieval motif. {ECO:0000269|PubMed:25122923}. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:21359175}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB14101.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB037765; BAA92582.2; -; mRNA. DR EMBL; CH471078; EAW65650.1; -; Genomic_DNA. DR EMBL; BC137081; AAI37082.1; -; mRNA. DR EMBL; BC137082; AAI37083.1; -; mRNA. DR EMBL; BC142650; AAI42651.1; -; mRNA. DR EMBL; BC150205; AAI50206.1; -; mRNA. DR EMBL; BC152428; AAI52429.1; -; mRNA. DR EMBL; AK022563; BAB14101.1; ALT_INIT; mRNA. DR CCDS; CCDS32083.1; -. DR RefSeq; NP_001153519.1; NM_001160047.1. DR RefSeq; NP_065835.2; NM_020784.3. DR AlphaFoldDB; Q9P2K2; -. DR SMR; Q9P2K2; -. DR BioGRID; 121602; 63. DR FunCoup; Q9P2K2; 728. DR IntAct; Q9P2K2; 53. DR STRING; 9606.ENSP00000281741; -. DR GlyCosmos; Q9P2K2; 1 site, No reported glycans. DR GlyGen; Q9P2K2; 1 site, 3 N-linked glycans (1 site). DR iPTMnet; Q9P2K2; -. DR PhosphoSitePlus; Q9P2K2; -. DR BioMuta; TXNDC16; -. DR DMDM; 212276524; -. DR jPOST; Q9P2K2; -. DR MassIVE; Q9P2K2; -. DR PaxDb; 9606-ENSP00000281741; -. DR PeptideAtlas; Q9P2K2; -. DR ProteomicsDB; 83828; -. DR Pumba; Q9P2K2; -. DR Antibodypedia; 149; 36 antibodies from 15 providers. DR DNASU; 57544; -. DR Ensembl; ENST00000281741.9; ENSP00000281741.4; ENSG00000087301.11. DR Ensembl; ENST00000936707.1; ENSP00000606766.1; ENSG00000087301.11. DR Ensembl; ENST00000956219.1; ENSP00000626278.1; ENSG00000087301.11. DR GeneID; 57544; -. DR KEGG; hsa:57544; -. DR MANE-Select; ENST00000281741.9; ENSP00000281741.4; NM_020784.3; NP_065835.2. DR UCSC; uc001wzs.4; human. DR AGR; HGNC:19965; -. DR ClinPGx; PA162407488; -. DR CTD; 57544; -. DR GeneCards; TXNDC16; -. DR HGNC; HGNC:19965; TXNDC16. DR HPA; ENSG00000087301; Low tissue specificity. DR MIM; 616179; gene. DR OpenTargets; ENSG00000087301; -. DR VEuPathDB; HostDB:ENSG00000087301; -. DR eggNOG; KOG0191; Eukaryota. DR GeneTree; ENSGT00390000006080; -. DR HOGENOM; CLU_018100_1_0_1; -. DR InParanoid; Q9P2K2; -. DR OMA; CRRTLMG; -. DR OrthoDB; 427280at2759; -. DR PAN-GO; Q9P2K2; 0 GO annotations based on evolutionary models. DR PhylomeDB; Q9P2K2; -. DR PathwayCommons; Q9P2K2; -. DR SignaLink; Q9P2K2; -. DR Agora; ENSG00000087301; -. DR BioGRID-ORCS; 57544; 10 hits in 1152 CRISPR screens. DR ChiTaRS; TXNDC16; human. DR GenomeRNAi; 57544; -. DR Pharos; Q9P2K2; Tdark. DR PRO; PR:Q9P2K2; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q9P2K2; protein. DR Bgee; ENSG00000087301; Expressed in seminal vesicle and 179 other cell types or tissues. DR ExpressionAtlas; Q9P2K2; baseline and differential. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR CDD; cd02961; PDI_a_family; 1. DR FunFam; 3.40.30.10:FF:000226; Thioredoxin domain containing 16; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR013766; Thioredoxin_domain. DR InterPro; IPR040090; TXNDC16. DR InterPro; IPR057642; TXNDC16_2nd. DR InterPro; IPR057645; TXNDC16_3rd. DR InterPro; IPR057639; TXNDC16_N. DR PANTHER; PTHR22699; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 16; 1. DR PANTHER; PTHR22699:SF1; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 16; 1. DR Pfam; PF00085; Thioredoxin; 1. DR Pfam; PF13848; Thioredoxin_6; 1. DR Pfam; PF24509; TXNDC16_2nd; 1. DR Pfam; PF24510; TXNDC16_3rd; 1. DR Pfam; PF24508; TXNDC16_N; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. PE 1: Evidence at protein level; KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; KW Proteomics identification; Reference proteome; Secreted; Signal. FT SIGNAL 1..27 FT /evidence="ECO:0000255, ECO:0000269|PubMed:25122923" FT CHAIN 28..825 FT /note="Thioredoxin domain-containing protein 16" FT /id="PRO_0000257789" FT DOMAIN 392..495 FT /note="Thioredoxin" FT REGION 762..787 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 816..819 FT /note="Mediates endoplasmic reticulum retention" FT /evidence="ECO:0000269|PubMed:25122923" FT COMPBIAS 767..787 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 460 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 449..456 FT /evidence="ECO:0000269|PubMed:21359175" FT VARIANT 136 FT /note="S -> N (in dbSNP:rs28759013)" FT /id="VAR_061899" FT VARIANT 152 FT /note="N -> Y (in dbSNP:rs28593180)" FT /id="VAR_061900" FT VARIANT 486 FT /note="E -> K (in dbSNP:rs7155490)" FT /evidence="ECO:0000269|PubMed:10718198, FT ECO:0000269|PubMed:15489334" FT /id="VAR_028919" FT CONFLICT 180 FT /note="A -> G (in Ref. 1; BAA92582)" FT /evidence="ECO:0000305" SQ SEQUENCE 825 AA; 93572 MW; B86F6DA47B5098D6 CRC64; MFSGFNVFRV GISFVIMCIF YMPTVNSLPE LSPQKYFSTL QPGKASLAYF CQADSPRTSV FLEELNEAVR PLQDYGISVA KVNCVKEEIS RYCGKEKDLM KAYLFKGNIL LREFPTDTLF DVNAIVAHVL FALLFSEVKY ITNLEDLQNI ENALKGKANI IFSYVRAIGI PEHRAVMEAA FVYGTTYQFV LTTEIALLES IGSEDVEYAH LYFFHCKLVL DLTQQCRRTL MEQPLTTLNI HLFIKTMKAP LLTEVAEDPQ QVSTVHLQLG LPLVFIVSQQ ATYEADRRTA EWVAWRLLGK AGVLLLLRDS LEVNIPQDAN VVFKRAEEGV PVEFLVLHDV DLIISHVENN MHIEEIQEDE DNDMEGPDID VQDDEVAETV FRDRKRKLPL ELTVELTEET FNATVMASDS IVLFYAGWQA VSMAFLQSYI DVAVKLKGTS TMLLTRINCA DWSDVCTKQN VTEFPIIKMY KKGENPVSYA GMLGTEDLLK FIQLNRISYP VNITSIQEAE EYLSGELYKD LILYSSVSVL GLFSPTMKTA KEDFSEAGNY LKGYVITGIY SEEDVLLLST KYAASLPALL LARHTEGKIE SIPLASTHAQ DIVQIITDAL LEMFPEITVE NLPSYFRLQK PLLILFSDGT VNPQYKKAIL TLVKQKYLDS FTPCWLNLKN TPVGRGILRA YFDPLPPLPL LVLVNLHSGG QVFAFPSDQA IIEENLVLWL KKLEAGLENH ITILPAQEWK PPLPAYDFLS MIDAATSQRG TRKVPKCMKE TDVQENDKEQ HEDKSAVRKE PIETLRIKHW NRSNWFKEAE KSFRRDKELG CSKVN //