ERP44_MOUSE
ID ERP44_MOUSE Reviewed; 406 AA.
AC Q9D1Q6; Q3TVI1; Q6A045;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
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;
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].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo;
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].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary 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).
RN [4]
RP INTERACTION WITH ITPR1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF CYS-58.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Mediates thiol-dependent retention in the early secretory
CC pathway, forming mixed disulfides with substrate proteins through its
CC conserved CRFS motif. Inhibits the calcium channel activity of ITPR1.
CC May have a role in the control of oxidative protein folding in the
CC endoplasmic reticulum. Required to retain ERO1A and ERO1B in the
CC endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9BS26}.
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 (By similarity). Directly
CC interacts with ITPR1 in a pH-, redox state- and calcium-dependent
CC manner, but not with ITPR2 or ITPR3 (PubMed:15652484). The strength of
CC this interaction inversely correlates with calcium concentration
CC (PubMed:15652484). {ECO:0000250|UniProtKB:Q9BS26,
CC ECO:0000269|PubMed:15652484}.
CC -!- INTERACTION:
CC Q9D1Q6; P11881: Itpr1; NbExp=5; IntAct=EBI-541567, EBI-541478;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:15652484}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15652484}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32251.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK003217; BAB22648.1; -; mRNA.
DR EMBL; AK151497; BAE30449.1; -; mRNA.
DR EMBL; AK160113; BAE35637.1; -; mRNA.
DR EMBL; AK172973; BAD32251.1; ALT_INIT; mRNA.
DR EMBL; BC019558; AAH19558.1; -; mRNA.
DR CCDS; CCDS18165.1; -.
DR RefSeq; NP_083848.1; NM_029572.2.
DR AlphaFoldDB; Q9D1Q6; -.
DR SMR; Q9D1Q6; -.
DR BioGRID; 218067; 33.
DR IntAct; Q9D1Q6; 17.
DR MINT; Q9D1Q6; -.
DR STRING; 10090.ENSMUSP00000030028; -.
DR iPTMnet; Q9D1Q6; -.
DR PhosphoSitePlus; Q9D1Q6; -.
DR SwissPalm; Q9D1Q6; -.
DR REPRODUCTION-2DPAGE; IPI00134058; -.
DR REPRODUCTION-2DPAGE; Q9D1Q6; -.
DR EPD; Q9D1Q6; -.
DR jPOST; Q9D1Q6; -.
DR MaxQB; Q9D1Q6; -.
DR PaxDb; Q9D1Q6; -.
DR PeptideAtlas; Q9D1Q6; -.
DR PRIDE; Q9D1Q6; -.
DR ProteomicsDB; 275477; -.
DR Antibodypedia; 753; 325 antibodies from 34 providers.
DR DNASU; 76299; -.
DR Ensembl; ENSMUST00000030028; ENSMUSP00000030028; ENSMUSG00000028343.
DR GeneID; 76299; -.
DR KEGG; mmu:76299; -.
DR UCSC; uc008suy.1; mouse.
DR CTD; 23071; -.
DR MGI; MGI:1923549; Erp44.
DR VEuPathDB; HostDB:ENSMUSG00000028343; -.
DR eggNOG; KOG0912; Eukaryota.
DR GeneTree; ENSGT00930000151031; -.
DR HOGENOM; CLU_054449_1_0_1; -.
DR InParanoid; Q9D1Q6; -.
DR OMA; IGKLGPC; -.
DR OrthoDB; 623253at2759; -.
DR PhylomeDB; Q9D1Q6; -.
DR TreeFam; TF106378; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 76299; 11 hits in 73 CRISPR screens.
DR ChiTaRS; Erp44; mouse.
DR PRO; PR:Q9D1Q6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D1Q6; protein.
DR Bgee; ENSMUSG00000028343; Expressed in seminal vesicle and 269 other tissues.
DR Genevisible; Q9D1Q6; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISS:UniProtKB.
DR GO; GO:0009100; P:glycoprotein metabolic process; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; ISS:UniProtKB.
DR CDD; cd03072; PDI_b'_ERp44; 1.
DR CDD; cd03070; PDI_b_ERp44; 1.
DR InterPro; IPR041862; ERp44_PDI_b.
DR InterPro; IPR041870; ERp44_PDI_b.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 3.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Disulfide bond; Endoplasmic reticulum; Reference proteome;
KW Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000250"
FT CHAIN 30..406
FT /note="Endoplasmic reticulum resident protein 44"
FT /id="PRO_0000034181"
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:0000269|PubMed:15652484"
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 189..241
FT /evidence="ECO:0000250"
FT DISULFID 301..318
FT /evidence="ECO:0000250"
FT MUTAGEN 58
FT /note="C->S: No effect on interaction with ITPR1."
FT /evidence="ECO:0000269|PubMed:15652484"
SQ SEQUENCE 406 AA; 46853 MW; F87935A5EB932927 CRC64;
MNPAVFLSLA DLRCSLLLLV TSIFTPITAE IASLDSENID EILNNADVAL VNFYADWCRF
SQMLHPIFEE ASDVIKEEYP DKNQVVFARV DCDQHSDIAQ RYRISKYPTL KLFRNGMMMK
REYRGQRSVK ALADYIRQQK SNPVHEIQSL DEVTNLDRSK RNIIGYFEQK DSENYRVFER
VASILHDDCA FLSAFGDLSK PERYNGDNVI YKPPGRSAPD MVYLGSMTNF DVTYNWIQDK
CVPLVREITF ENGEELTEEG LPFLILFHMK DDTESLEIFQ NEVARQLISE KGTINFLHAD
CDKFRHPLLH IQKTPADCPV IAIDSFRHMY VFGDFKDVLI PGKLKQFVFD LHSGKLHREF
HHGPDPTDTA PGEQDQDVAS SPPESSFQKL APSEYRYTLL RDRDEL
