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Q9D1Q6 (ERP44_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoplasmic reticulum resident protein 44

Short name=ER protein 44
Short name=ERp44
Alternative name(s):
Thioredoxin domain-containing protein 4
Gene names
Name:Erp44
Synonyms:Kiaa0573, Txndc4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.4

Subcellular location

Endoplasmic reticulum lumen Ref.4.

Tissue specificity

Widely expressed. Ref.4

Sequence similarities

Contains 1 thioredoxin domain.

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Itpr1P118815EBI-541567,EBI-541478

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 By similarity
Chain30 – 406377Endoplasmic reticulum resident protein 44
PRO_0000034181

Regions

Domain30 – 138109Thioredoxin
Region236 – 28550Interaction with ITPR1
Motif403 – 4064Prevents secretion from ER Potential

Amino acid modifications

Disulfide bond189 ↔ 241 By similarity
Disulfide bond301 ↔ 318 By similarity

Experimental info

Mutagenesis581C → S: No effect on interaction with ITPR1. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9D1Q6 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F87935A5EB932927

FASTA40646,853
        10         20         30         40         50         60 
MNPAVFLSLA DLRCSLLLLV TSIFTPITAE IASLDSENID EILNNADVAL VNFYADWCRF 

        70         80         90        100        110        120 
SQMLHPIFEE ASDVIKEEYP DKNQVVFARV DCDQHSDIAQ RYRISKYPTL KLFRNGMMMK 

       130        140        150        160        170        180 
REYRGQRSVK ALADYIRQQK SNPVHEIQSL DEVTNLDRSK RNIIGYFEQK DSENYRVFER 

       190        200        210        220        230        240 
VASILHDDCA FLSAFGDLSK PERYNGDNVI YKPPGRSAPD MVYLGSMTNF DVTYNWIQDK 

       250        260        270        280        290        300 
CVPLVREITF ENGEELTEEG LPFLILFHMK DDTESLEIFQ NEVARQLISE KGTINFLHAD 

       310        320        330        340        350        360 
CDKFRHPLLH IQKTPADCPV IAIDSFRHMY VFGDFKDVLI PGKLKQFVFD LHSGKLHREF 

       370        380        390        400 
HHGPDPTDTA PGEQDQDVAS SPPESSFQKL APSEYRYTLL RDRDEL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_083848.1. NM_029572.2.
UniGeneMm.317701.

3D structure databases

ProteinModelPortalQ9D1Q6.
SMRQ9D1Q6. Positions 33-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9D1Q6. 9 interactions.
MINTMINT-4998069.
STRING10090.ENSMUSP00000030028.

2D gel databases

REPRODUCTION-2DPAGEIPI00134058.
Q9D1Q6.

Proteomic databases

PaxDbQ9D1Q6.
PRIDEQ9D1Q6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030028; ENSMUSP00000030028; ENSMUSG00000028343.
GeneID76299.
KEGGmmu:76299.
UCSCuc008suy.1. mouse.

Organism-specific databases

CTD23071.
MGIMGI:1923549. Erp44.
RougeSearch...

Phylogenomic databases

eggNOGCOG0526.
GeneTreeENSGT00740000115037.
HOGENOMHOG000007707.
InParanoidQ9D1Q6.
KOK17264.
OMARHMYLFP.
OrthoDBEOG718KCX.
PhylomeDBQ9D1Q6.
TreeFamTF106378.

Gene expression databases

BgeeQ9D1Q6.
GenevestigatorQ9D1Q6.

Family and domain databases

Gene3D3.40.30.10. 2 hits.
InterProIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 3 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio344925.
PROQ9D1Q6.
SOURCESearch...

Entry information

Entry nameERP44_MOUSE
AccessionPrimary (citable) accession number: Q9D1Q6
Secondary accession number(s): Q3TVI1, Q6A045
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot