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Protein

Endoplasmic reticulum resident protein 44

Gene

Erp44

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1L and ERO1LB in the endoplasmic reticulum (By similarity).By similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. glycoprotein metabolic process Source: UniProtKB
  3. protein folding Source: UniProtKB
  4. response to endoplasmic reticulum stress Source: UniProtKB
  5. response to unfolded protein Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmic reticulum resident protein 44
Short name:
ER protein 44
Short name:
ERp44
Alternative name(s):
Thioredoxin domain-containing protein 4
Gene namesi
Name:Erp44
Synonyms:Kiaa0573, Txndc4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1923549. Erp44.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

  1. cell surface Source: MGI
  2. endoplasmic reticulum Source: GO_Central
  3. endoplasmic reticulum-Golgi intermediate compartment Source: MGI
  4. endoplasmic reticulum lumen Source: UniProtKB
  5. endoplasmic reticulum membrane Source: UniProtKB
  6. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581C → S: No effect on interaction with ITPR1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929By similarityAdd
BLAST
Chaini30 – 406377Endoplasmic reticulum resident protein 44PRO_0000034181Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi189 ↔ 241By similarity
Disulfide bondi301 ↔ 318By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ9D1Q6.
PaxDbiQ9D1Q6.
PRIDEiQ9D1Q6.

2D gel databases

REPRODUCTION-2DPAGEIPI00134058.
Q9D1Q6.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ9D1Q6.
GenevestigatoriQ9D1Q6.

Interactioni

Subunit structurei

Forms mixed disulfides with both ERO1L and ERO1LB and cargo folding intermediates (By similarity). Directly interacts with ITPR1 in a pH-, redox state- and calcium-dependent manner, but not with ITPR2 or ITPR3. The strength of this interaction inversely correlates with calcium concentration.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Itpr1P118815EBI-541567,EBI-541478

Protein-protein interaction databases

IntActiQ9D1Q6. 9 interactions.
MINTiMINT-4998069.
STRINGi10090.ENSMUSP00000030028.

Structurei

3D structure databases

ProteinModelPortaliQ9D1Q6.
SMRiQ9D1Q6. Positions 33-401.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 138109ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni236 – 28550Interaction with ITPR1Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi403 – 4064Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000007707.
InParanoidiQ9D1Q6.
KOiK17264.
OMAiRHMYLFP.
OrthoDBiEOG718KCX.
PhylomeDBiQ9D1Q6.
TreeFamiTF106378.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 3 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D1Q6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPAVFLSLA DLRCSLLLLV TSIFTPITAE IASLDSENID EILNNADVAL
60 70 80 90 100
VNFYADWCRF SQMLHPIFEE ASDVIKEEYP DKNQVVFARV DCDQHSDIAQ
110 120 130 140 150
RYRISKYPTL KLFRNGMMMK REYRGQRSVK ALADYIRQQK SNPVHEIQSL
160 170 180 190 200
DEVTNLDRSK RNIIGYFEQK DSENYRVFER VASILHDDCA FLSAFGDLSK
210 220 230 240 250
PERYNGDNVI YKPPGRSAPD MVYLGSMTNF DVTYNWIQDK CVPLVREITF
260 270 280 290 300
ENGEELTEEG LPFLILFHMK DDTESLEIFQ NEVARQLISE KGTINFLHAD
310 320 330 340 350
CDKFRHPLLH IQKTPADCPV IAIDSFRHMY VFGDFKDVLI PGKLKQFVFD
360 370 380 390 400
LHSGKLHREF HHGPDPTDTA PGEQDQDVAS SPPESSFQKL APSEYRYTLL

RDRDEL
Length:406
Mass (Da):46,853
Last modified:June 1, 2001 - v1
Checksum:iF87935A5EB932927
GO

Sequence cautioni

The sequence BAD32251.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003217 mRNA. Translation: BAB22648.1.
AK151497 mRNA. Translation: BAE30449.1.
AK160113 mRNA. Translation: BAE35637.1.
AK172973 mRNA. Translation: BAD32251.1. Different initiation.
BC019558 mRNA. Translation: AAH19558.1.
CCDSiCCDS18165.1.
RefSeqiNP_083848.1. NM_029572.2.
UniGeneiMm.317701.

Genome annotation databases

EnsembliENSMUST00000030028; ENSMUSP00000030028; ENSMUSG00000028343.
GeneIDi76299.
KEGGimmu:76299.
UCSCiuc008suy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003217 mRNA. Translation: BAB22648.1.
AK151497 mRNA. Translation: BAE30449.1.
AK160113 mRNA. Translation: BAE35637.1.
AK172973 mRNA. Translation: BAD32251.1. Different initiation.
BC019558 mRNA. Translation: AAH19558.1.
CCDSiCCDS18165.1.
RefSeqiNP_083848.1. NM_029572.2.
UniGeneiMm.317701.

3D structure databases

ProteinModelPortaliQ9D1Q6.
SMRiQ9D1Q6. Positions 33-401.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D1Q6. 9 interactions.
MINTiMINT-4998069.
STRINGi10090.ENSMUSP00000030028.

2D gel databases

REPRODUCTION-2DPAGEIPI00134058.
Q9D1Q6.

Proteomic databases

MaxQBiQ9D1Q6.
PaxDbiQ9D1Q6.
PRIDEiQ9D1Q6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030028; ENSMUSP00000030028; ENSMUSG00000028343.
GeneIDi76299.
KEGGimmu:76299.
UCSCiuc008suy.1. mouse.

Organism-specific databases

CTDi23071.
MGIiMGI:1923549. Erp44.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000007707.
InParanoidiQ9D1Q6.
KOiK17264.
OMAiRHMYLFP.
OrthoDBiEOG718KCX.
PhylomeDBiQ9D1Q6.
TreeFamiTF106378.

Miscellaneous databases

NextBioi344925.
PROiQ9D1Q6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D1Q6.
GenevestigatoriQ9D1Q6.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 3 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow and Embryo.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Salivary gland.
  4. "Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44."
    Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T., Mikoshiba K.
    Cell 120:85-98(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ITPR1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-58.

Entry informationi

Entry nameiERP44_MOUSE
AccessioniPrimary (citable) accession number: Q9D1Q6
Secondary accession number(s): Q3TVI1, Q6A045
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.