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Q9D1Q6

- ERP44_MOUSE

UniProt

Q9D1Q6 - ERP44_MOUSE

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
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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 binding Source: IntAct
    2. 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

    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

    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.
    GeneTreeiENSGT00740000115037.
    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.

    Q9D1Q6-1 [UniParc]FASTAAdd to Basket

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    MNPAVFLSLA DLRCSLLLLV TSIFTPITAE IASLDSENID EILNNADVAL    50
    VNFYADWCRF SQMLHPIFEE ASDVIKEEYP DKNQVVFARV DCDQHSDIAQ 100
    RYRISKYPTL KLFRNGMMMK REYRGQRSVK ALADYIRQQK SNPVHEIQSL 150
    DEVTNLDRSK RNIIGYFEQK DSENYRVFER VASILHDDCA FLSAFGDLSK 200
    PERYNGDNVI YKPPGRSAPD MVYLGSMTNF DVTYNWIQDK CVPLVREITF 250
    ENGEELTEEG LPFLILFHMK DDTESLEIFQ NEVARQLISE KGTINFLHAD 300
    CDKFRHPLLH IQKTPADCPV IAIDSFRHMY VFGDFKDVLI PGKLKQFVFD 350
    LHSGKLHREF HHGPDPTDTA PGEQDQDVAS SPPESSFQKL APSEYRYTLL 400
    RDRDEL 406
    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 ENSGT00740000115037.
    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

    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 1, 2014
    This is version 110 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