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Q9D1Q6

- ERP44_MOUSE

UniProt

Q9D1Q6 - ERP44_MOUSE

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Protein

Endoplasmic reticulum resident protein 44

Gene

Erp44

Organism
Mus musculus (Mouse)
Status
Reviewed - 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: Chromosome 4

Organism-specific databases

MGIiMGI:1923549. Erp44.

Subcellular locationi

Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. cell surface Source: MGI
  2. endoplasmic reticulum Source: RefGenome
  3. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
  4. endoplasmic reticulum lumen Source: UniProtKB
  5. endoplasmic reticulum membrane Source: UniProtKB
  6. extracellular vesicular exosome Source: Ensembl
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.
OMAiENAPDMV.
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 [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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS18165.1.
RefSeqi NP_083848.1. NM_029572.2.
UniGenei Mm.317701.

3D structure databases

ProteinModelPortali Q9D1Q6.
SMRi Q9D1Q6. Positions 33-401.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9D1Q6. 9 interactions.
MINTi MINT-4998069.
STRINGi 10090.ENSMUSP00000030028.

2D gel databases

REPRODUCTION-2DPAGE IPI00134058.
Q9D1Q6.

Proteomic databases

MaxQBi Q9D1Q6.
PaxDbi Q9D1Q6.
PRIDEi Q9D1Q6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030028 ; ENSMUSP00000030028 ; ENSMUSG00000028343 .
GeneIDi 76299.
KEGGi mmu:76299.
UCSCi uc008suy.1. mouse.

Organism-specific databases

CTDi 23071.
MGIi MGI:1923549. Erp44.
Rougei Search...

Phylogenomic databases

eggNOGi COG0526.
GeneTreei ENSGT00760000119201.
HOGENOMi HOG000007707.
InParanoidi Q9D1Q6.
KOi K17264.
OMAi ENAPDMV.
OrthoDBi EOG718KCX.
PhylomeDBi Q9D1Q6.
TreeFami TF106378.

Miscellaneous databases

NextBioi 344925.
PROi Q9D1Q6.
SOURCEi Search...

Gene expression databases

Bgeei Q9D1Q6.
Genevestigatori Q9D1Q6.

Family and domain databases

Gene3Di 3.40.30.10. 2 hits.
InterProi IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 1 hit.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 3 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(2005) [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(2004) [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(2004) [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(2005) [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: October 29, 2014
This is version 111 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