ID   ERP44_HUMAN             Reviewed;         406 AA.
AC   Q9BS26; O60319; Q4VXC1; Q5VWZ7; Q6UW14; Q8WX67;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=Endoplasmic reticulum resident protein 44;
DE            Short=ER protein 44;
DE            Short=ERp44;
DE   AltName: Full=Thioredoxin domain-containing protein 4;
DE   Flags: Precursor;
GN   Name=ERP44; Synonyms=KIAA0573, TXNDC4; ORFNames=UNQ532/PRO1075;
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 [MRNA], PROTEIN SEQUENCE OF 149-158 AND 314-327,
RP   FUNCTION, INTERACTION WITH ERO1A AND ERO1B, MIXED DISULFIDE BOND FORMATION,
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RC   TISSUE=Cervix;
RX   PubMed=11847130; DOI=10.1093/emboj/21.4.835;
RA   Anelli T., Alessio M., Mezghrani A., Simmen T., Talamo F., Bachi A.,
RA   Sitia R.;
RT   "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin
RT   family.";
RL   EMBO J. 21:835-844(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA   Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA   Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. IX. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:31-39(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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   [7]
RP   FUNCTION.
RX   PubMed=14517240; DOI=10.1093/emboj/cdg491;
RA   Anelli T., Alessio M., Bachi A., Bergamelli L., Bertoli G., Camerini S.,
RA   Mezghrani A., Ruffato E., Simmen T., Sitia R.;
RT   "Thiol-mediated protein retention in the endoplasmic reticulum: the role of
RT   ERp44.";
RL   EMBO J. 22:5015-5022(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Platelet;
RX   PubMed=11921445;
RX   DOI=10.1002/1615-9861(200203)2:3<288::aid-prot288>3.0.co;2-0;
RA   O'Neill E.E., Brock C.J., von Kriegsheim A.F., Pearce A.C., Dwek R.A.,
RA   Watson S.P., Hebestreit H.F.;
RT   "Towards complete analysis of the platelet proteome.";
RL   Proteomics 2:288-305(2002).
RN   [9]
RP   FUNCTION, INTERACTION WITH ITPR1, AND SUBCELLULAR LOCATION.
RX   PubMed=15652484; DOI=10.1016/j.cell.2004.11.048;
RA   Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T., Mikoshiba K.;
RT   "Subtype-specific and ER lumenal environment-dependent regulation of
RT   inositol 1,4,5-trisphosphate receptor type 1 by ERp44.";
RL   Cell 120:85-98(2005).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [13]
RP   FUNCTION, AND INTERACTION WITH ERO1A.
RX   PubMed=29858230; DOI=10.15252/embj.201798699;
RA   Zhang J., Zhu Q., Wang X., Yu J., Chen X., Wang J., Wang X., Xiao J.,
RA   Wang C.C., Wang L.;
RT   "Secretory kinase Fam20C tunes endoplasmic reticulum redox state via
RT   phosphorylation of Ero1alpha.";
RL   EMBO J. 37:0-0(2018).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-406, AND DISULFIDE BONDS.
RX   PubMed=18552768; DOI=10.1038/embor.2008.88;
RA   Wang L., Wang L., Vavassori S., Li S., Ke H., Anelli T., Degano M.,
RA   Ronzoni R., Sitia R., Sun F., Wang C.-C.;
RT   "Crystal structure of human ERp44 shows a dynamic functional modulation by
RT   its carboxy-terminal tail.";
RL   EMBO Rep. 9:642-647(2008).
CC   -!- FUNCTION: Mediates thiol-dependent retention in the early secretory
CC       pathway, forming mixed disulfides with substrate proteins through its
CC       conserved CRFS motif (PubMed:11847130, PubMed:14517240). Inhibits the
CC       calcium channel activity of ITPR1 (PubMed:15652484). May have a role in
CC       the control of oxidative protein folding in the endoplasmic reticulum
CC       (PubMed:11847130, PubMed:29858230, PubMed:14517240). Required to retain
CC       ERO1A and ERO1B in the endoplasmic reticulum (PubMed:11847130,
CC       PubMed:29858230). {ECO:0000269|PubMed:11847130,
CC       ECO:0000269|PubMed:14517240, ECO:0000269|PubMed:15652484,
CC       ECO:0000269|PubMed:29858230}.
CC   -!- SUBUNIT: Forms mixed disulfides with both ERO1A and ERO1B and cargo
CC       folding intermediates; the interactions with ERO1A and ERO1B result in
CC       their retention in the endoplasmic reticulum (PubMed:11847130,
CC       PubMed:29858230). Directly interacts with ITPR1 in a pH-, redox
CC       state- and calcium-dependent manner, but not with ITPR2 or ITPR3
CC       (PubMed:15652484). The strength of this interaction inversely
CC       correlates with calcium concentration (By similarity).
CC       {ECO:0000250|UniProtKB:Q9D1Q6, ECO:0000269|PubMed:11847130,
CC       ECO:0000269|PubMed:15652484, ECO:0000269|PubMed:29858230}.
CC   -!- INTERACTION:
CC       Q9BS26; Q06481-5: APLP2; NbExp=3; IntAct=EBI-541644, EBI-25646567;
CC       Q9BS26; P05067: APP; NbExp=3; IntAct=EBI-541644, EBI-77613;
CC       Q9BS26; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-541644, EBI-9087876;
CC       Q9BS26; P49257: LMAN1; NbExp=3; IntAct=EBI-541644, EBI-1057738;
CC       Q9BS26; P07948: LYN; NbExp=3; IntAct=EBI-541644, EBI-79452;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000269|PubMed:11847130, ECO:0000269|PubMed:15652484}.
CC   -!- INDUCTION: Up-regulated by inducers of the unfolded protein response
CC       (UPR), including tunicamycin and dithiothreitol.
CC       {ECO:0000269|PubMed:11847130}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA25499.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ344330; CAC87611.1; -; mRNA.
DR   EMBL; AB011145; BAA25499.1; ALT_INIT; mRNA.
DR   EMBL; AY359048; AAQ89407.1; -; mRNA.
DR   EMBL; AK075024; BAG52054.1; -; mRNA.
DR   EMBL; AL360084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL137072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL358937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005374; AAH05374.1; -; mRNA.
DR   CCDS; CCDS35082.1; -.
DR   RefSeq; NP_055866.1; NM_015051.2.
DR   PDB; 2R2J; X-ray; 2.60 A; A=30-406.
DR   PDB; 5GU6; X-ray; 2.00 A; A=30-402.
DR   PDB; 5GU7; X-ray; 2.05 A; C=30-402.
DR   PDB; 5HQP; X-ray; 2.60 A; C/D=30-406.
DR   PDB; 5XWM; X-ray; 2.45 A; A/B/C/D=30-406.
DR   PDBsum; 2R2J; -.
DR   PDBsum; 5GU6; -.
DR   PDBsum; 5GU7; -.
DR   PDBsum; 5HQP; -.
DR   PDBsum; 5XWM; -.
DR   AlphaFoldDB; Q9BS26; -.
DR   SMR; Q9BS26; -.
DR   BioGRID; 116704; 192.
DR   IntAct; Q9BS26; 84.
DR   MINT; Q9BS26; -.
DR   STRING; 9606.ENSP00000262455; -.
DR   GlyCosmos; Q9BS26; 4 sites, 5 glycans.
DR   GlyGen; Q9BS26; 9 sites, 6 O-linked glycans (9 sites).
DR   iPTMnet; Q9BS26; -.
DR   MetOSite; Q9BS26; -.
DR   PhosphoSitePlus; Q9BS26; -.
DR   SwissPalm; Q9BS26; -.
DR   BioMuta; ERP44; -.
DR   DMDM; 31077035; -.
DR   REPRODUCTION-2DPAGE; IPI00401264; -.
DR   CPTAC; CPTAC-363; -.
DR   CPTAC; CPTAC-364; -.
DR   EPD; Q9BS26; -.
DR   jPOST; Q9BS26; -.
DR   MassIVE; Q9BS26; -.
DR   MaxQB; Q9BS26; -.
DR   PaxDb; 9606-ENSP00000262455; -.
DR   PeptideAtlas; Q9BS26; -.
DR   ProteomicsDB; 78861; -.
DR   Pumba; Q9BS26; -.
DR   Antibodypedia; 753; 351 antibodies from 34 providers.
DR   DNASU; 23071; -.
DR   Ensembl; ENST00000262455.7; ENSP00000262455.6; ENSG00000023318.9.
DR   GeneID; 23071; -.
DR   KEGG; hsa:23071; -.
DR   MANE-Select; ENST00000262455.7; ENSP00000262455.6; NM_015051.3; NP_055866.1.
DR   UCSC; uc004bam.4; human.
DR   AGR; HGNC:18311; -.
DR   CTD; 23071; -.
DR   DisGeNET; 23071; -.
DR   GeneCards; ERP44; -.
DR   HGNC; HGNC:18311; ERP44.
DR   HPA; ENSG00000023318; Low tissue specificity.
DR   MIM; 609170; gene.
DR   neXtProt; NX_Q9BS26; -.
DR   OpenTargets; ENSG00000023318; -.
DR   PharmGKB; PA164719295; -.
DR   VEuPathDB; HostDB:ENSG00000023318; -.
DR   eggNOG; KOG0912; Eukaryota.
DR   GeneTree; ENSGT00930000151031; -.
DR   HOGENOM; CLU_054449_1_0_1; -.
DR   InParanoid; Q9BS26; -.
DR   OMA; DWCRFSN; -.
DR   OrthoDB; 90290at2759; -.
DR   PhylomeDB; Q9BS26; -.
DR   TreeFam; TF106378; -.
DR   PathwayCommons; Q9BS26; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; Q9BS26; -.
DR   SIGNOR; Q9BS26; -.
DR   BioGRID-ORCS; 23071; 32 hits in 1174 CRISPR screens.
DR   ChiTaRS; ERP44; human.
DR   EvolutionaryTrace; Q9BS26; -.
DR   GeneWiki; ERP44; -.
DR   GenomeRNAi; 23071; -.
DR   Pharos; Q9BS26; Tbio.
DR   PRO; PR:Q9BS26; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q9BS26; Protein.
DR   Bgee; ENSG00000023318; Expressed in type B pancreatic cell and 216 other cell types or tissues.
DR   ExpressionAtlas; Q9BS26; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IDA:UniProtKB.
DR   GO; GO:0045454; P:cell redox homeostasis; TAS:UniProtKB.
DR   GO; GO:0009100; P:glycoprotein metabolic process; IDA:UniProtKB.
DR   GO; GO:0006457; P:protein folding; IDA:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR   GO; GO:0006986; P:response to unfolded protein; IDA:UniProtKB.
DR   CDD; cd02996; PDI_a_ERp44; 1.
DR   CDD; cd03072; PDI_b'_ERp44; 1.
DR   CDD; cd03070; PDI_b_ERp44; 1.
DR   DisProt; DP02173; -.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR   InterPro; IPR041862; ERp44_PDI_b.
DR   InterPro; IPR041870; ERp44_PDI_b.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR46295; ENDOPLASMIC RETICULUM RESIDENT PROTEIN 44; 1.
DR   PANTHER; PTHR46295:SF1; ENDOPLASMIC RETICULUM RESIDENT PROTEIN 44; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 3.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
DR   Genevisible; Q9BS26; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Direct protein sequencing; Disulfide bond;
KW   Endoplasmic reticulum; Reference proteome; Signal; Stress response.
FT   SIGNAL          1..29
FT   CHAIN           30..406
FT                   /note="Endoplasmic reticulum resident protein 44"
FT                   /id="PRO_0000034180"
FT   DOMAIN          30..138
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          236..285
FT                   /note="Interaction with ITPR1"
FT                   /evidence="ECO:0000250"
FT   REGION          360..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           403..406
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   COMPBIAS        373..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        58
FT                   /note="Interchain (with ERO1A)"
FT                   /evidence="ECO:0000269|PubMed:18552768"
FT   DISULFID        189..241
FT                   /evidence="ECO:0000269|PubMed:18552768"
FT   DISULFID        301..318
FT                   /evidence="ECO:0000269|PubMed:18552768"
FT   CONFLICT        35
FT                   /note="D -> A (in Ref. 3; AAQ89407)"
FT                   /evidence="ECO:0000305"
FT   STRAND          30..33
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   TURN            36..38
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           39..45
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          47..54
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           59..78
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:5HQP"
FT   STRAND          86..91
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   TURN            92..94
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           96..101
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          106..114
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          117..122
FT                   /evidence="ECO:0007829|PDB:5GU7"
FT   HELIX           129..140
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:2R2J"
FT   HELIX           151..154
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          158..160
FT                   /evidence="ECO:0007829|PDB:5HQP"
FT   STRAND          162..166
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          170..172
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           173..185
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   TURN            186..188
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          189..194
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           196..199
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           200..202
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          206..212
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          214..218
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           230..241
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          244..247
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   TURN            250..252
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           253..258
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          263..268
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           273..286
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           288..290
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   TURN            291..293
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          294..300
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   TURN            301..303
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           305..310
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           315..317
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          319..324
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          326..331
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           335..339
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           343..352
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           355..362
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   HELIX           387..390
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   TURN            394..396
FT                   /evidence="ECO:0007829|PDB:5GU6"
FT   STRAND          397..400
FT                   /evidence="ECO:0007829|PDB:5GU6"
SQ   SEQUENCE   406 AA;  46971 MW;  3865DCF3811BC263 CRC64;
     MHPAVFLSLP DLRCSLLLLV TWVFTPVTTE ITSLDTENID EILNNADVAL VNFYADWCRF
     SQMLHPIFEE ASDVIKEEFP NENQVVFARV DCDQHSDIAQ RYRISKYPTL KLFRNGMMMK
     REYRGQRSVK ALADYIRQQK SDPIQEIRDL AEITTLDRSK RNIIGYFEQK DSDNYRVFER
     VANILHDDCA FLSAFGDVSK PERYSGDNII YKPPGHSAPD MVYLGAMTNF DVTYNWIQDK
     CVPLVREITF ENGEELTEEG LPFLILFHMK EDTESLEIFQ NEVARQLISE KGTINFLHAD
     CDKFRHPLLH IQKTPADCPV IAIDSFRHMY VFGDFKDVLI PGKLKQFVFD LHSGKLHREF
     HHGPDPTDTA PGEQAQDVAS SPPESSFQKL APSEYRYTLL RDRDEL
//