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P49222

- EPB42_MOUSE

UniProt

P49222 - EPB42_MOUSE

Protein

Erythrocyte membrane protein band 4.2

Gene

Epb42

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Probably plays an important role in the regulation of erythrocyte shape and mechanical properties.

    GO - Molecular functioni

    1. protein-glutamine gamma-glutamyltransferase activity Source: InterPro

    GO - Biological processi

    1. cell morphogenesis Source: MGI
    2. erythrocyte maturation Source: UniProtKB-KW
    3. hemoglobin metabolic process Source: MGI
    4. ion homeostasis Source: MGI
    5. iron ion homeostasis Source: MGI
    6. peptide cross-linking Source: InterPro
    7. regulation of cell shape Source: UniProtKB-KW
    8. spleen development Source: MGI

    Keywords - Biological processi

    Cell shape, Erythrocyte maturation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Erythrocyte membrane protein band 4.2
    Short name:
    Erythrocyte protein 4.2
    Short name:
    P4.2
    Gene namesi
    Name:Epb42
    Synonyms:Epb4.2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:95402. Epb4.2.

    Subcellular locationi

    Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmcytoskeleton
    Note: Cytoplasmic surface of erythrocyte membranes.

    GO - Cellular componenti

    1. cortical cytoskeleton Source: MGI
    2. membrane Source: MGI
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 691690Erythrocyte membrane protein band 4.2PRO_0000213721Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity

    Keywords - PTMi

    Lipoprotein, Myristate

    Proteomic databases

    MaxQBiP49222.
    PaxDbiP49222.
    PRIDEiP49222.

    PTM databases

    PhosphoSiteiP49222.

    Expressioni

    Gene expression databases

    ArrayExpressiP49222.
    BgeeiP49222.
    CleanExiMM_EPB4.2.
    GenevestigatoriP49222.

    Interactioni

    Subunit structurei

    Oligomer. Interacts with the cytoplasmic domain of SLC4A1/band 3 anion transport protein.

    Protein-protein interaction databases

    IntActiP49222. 2 interactions.
    MINTiMINT-4094485.

    Structurei

    3D structure databases

    ProteinModelPortaliP49222.
    SMRiP49222. Positions 5-684.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni31 – 399Band 3 bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG87163.
    GeneTreeiENSGT00740000115034.
    HOGENOMiHOG000231695.
    HOVERGENiHBG106048.
    InParanoidiQ3UP33.
    OMAiSCFAQED.
    OrthoDBiEOG7Z0JVS.
    TreeFamiTF324278.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    3.90.260.10. 1 hit.
    InterProiIPR023608. Gln_gamma-glutamylTfrase_euk.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002931. Transglutaminase-like.
    IPR008958. Transglutaminase_C.
    IPR013808. Transglutaminase_CS.
    IPR001102. Transglutaminase_N.
    [Graphical view]
    PANTHERiPTHR11590. PTHR11590. 1 hit.
    PfamiPF00927. Transglut_C. 2 hits.
    PF01841. Transglut_core. 1 hit.
    PF00868. Transglut_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000459. TGM_EBP42. 1 hit.
    SMARTiSM00460. TGc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49309. SSF49309. 2 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS00547. TRANSGLUTAMINASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P49222-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGQALSIKSC DFHAAENNEE HYTKAISSQH LTLRRGQSFT ITLNFRAPTH    50
    TFLSALKKVA LIAQTGEQPS KINKTQAIFP ISSLGDQKGW SAAVEERDAQ 100
    HWTVSVTTPV DAVIGHYSLL LQVSGKKQYP LGQFTLLFNP WNRDDAVFLQ 150
    NEAERTEYVL NQNGFIYLGT ADCIQEEPWD FGQFEKDVMD LSLKLLSMDK 200
    QVKDWNQPAH VARVVGALLH ALKKKSVLPI SQTQAAQEGA LLYKRRGSVP 250
    ILRQWLTGQG RAVYETQAWV SAAVACTVLR CLGIPARVVT TFDSAQGTVG 300
    SLLVDEYYNE EGLQNGEGQR GHIWVFQTSV ECWMNRPDLS QGYGGWQILH 350
    PRAPNGAGVL GSCSLVPVRA VKEGELQLDP AVPELFAAVN ASCVVWKCCE 400
    DGKLELTNSN RKDVGNCIST KVVGSDRCED ITQNYKYPAG SLQEKEVLEK 450
    VQKERLKLGK DNGMCPPSCE PWDPLHMFFE ASSSIPLSGD GQLSVTLINP 500
    TDEEKKVHLV IGAQALYYNG VLAAGLWSKK QLFMLKPNQV MRLSTNLSFS 550
    CFEQTPPENS FLRVTAMARY SHTSLSCFAQ ENMAIGKPDL IIEMPKRAAQ 600
    YRPLTVSVRM HNSLEAPMQN CIISIFGRGL IHREKRYGLG SLWPGSSLHT 650
    QFQFTPTHLG LQRLTVEVDC DMFQNLTGYR SVLVVAPEVS V 691
    Length:691
    Mass (Da):76,756
    Last modified:July 27, 2011 - v3
    Checksum:i433E1623971D60C3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221Y → H in AAA67917. (PubMed:7959722)Curated
    Sequence conflicti224 – 2241K → N in AAA67917. (PubMed:7959722)Curated
    Sequence conflicti398 – 3981C → S in AAA67917. (PubMed:7959722)Curated
    Sequence conflicti450 – 4501K → R in AAA67917. (PubMed:7959722)Curated
    Sequence conflicti528 – 5281S → R in AAA67917. (PubMed:7959722)Curated
    Sequence conflicti621 – 6211C → S in AAA62275. (PubMed:7919657)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03487 mRNA. Translation: AAA62275.1.
    U04055 mRNA. Translation: AAA67916.1.
    U04056 Genomic DNA. Translation: AAA67917.1.
    L35933 mRNA. Translation: AAA39875.1.
    AK143841 mRNA. Translation: BAE25564.1.
    AL844548 Genomic DNA. Translation: CAM19015.1.
    CCDSiCCDS16631.1.
    PIRiA54741.
    RefSeqiNP_038541.1. NM_013513.2.
    UniGeneiMm.240051.

    Genome annotation databases

    EnsembliENSMUST00000102490; ENSMUSP00000099548; ENSMUSG00000023216.
    GeneIDi13828.
    KEGGimmu:13828.
    UCSCiuc008lxi.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03487 mRNA. Translation: AAA62275.1 .
    U04055 mRNA. Translation: AAA67916.1 .
    U04056 Genomic DNA. Translation: AAA67917.1 .
    L35933 mRNA. Translation: AAA39875.1 .
    AK143841 mRNA. Translation: BAE25564.1 .
    AL844548 Genomic DNA. Translation: CAM19015.1 .
    CCDSi CCDS16631.1.
    PIRi A54741.
    RefSeqi NP_038541.1. NM_013513.2.
    UniGenei Mm.240051.

    3D structure databases

    ProteinModelPortali P49222.
    SMRi P49222. Positions 5-684.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P49222. 2 interactions.
    MINTi MINT-4094485.

    PTM databases

    PhosphoSitei P49222.

    Proteomic databases

    MaxQBi P49222.
    PaxDbi P49222.
    PRIDEi P49222.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000102490 ; ENSMUSP00000099548 ; ENSMUSG00000023216 .
    GeneIDi 13828.
    KEGGi mmu:13828.
    UCSCi uc008lxi.1. mouse.

    Organism-specific databases

    CTDi 13828.
    MGIi MGI:95402. Epb4.2.

    Phylogenomic databases

    eggNOGi NOG87163.
    GeneTreei ENSGT00740000115034.
    HOGENOMi HOG000231695.
    HOVERGENi HBG106048.
    InParanoidi Q3UP33.
    OMAi SCFAQED.
    OrthoDBi EOG7Z0JVS.
    TreeFami TF324278.

    Miscellaneous databases

    NextBioi 284632.
    PROi P49222.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49222.
    Bgeei P49222.
    CleanExi MM_EPB4.2.
    Genevestigatori P49222.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    3.90.260.10. 1 hit.
    InterProi IPR023608. Gln_gamma-glutamylTfrase_euk.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002931. Transglutaminase-like.
    IPR008958. Transglutaminase_C.
    IPR013808. Transglutaminase_CS.
    IPR001102. Transglutaminase_N.
    [Graphical view ]
    PANTHERi PTHR11590. PTHR11590. 1 hit.
    Pfami PF00927. Transglut_C. 2 hits.
    PF01841. Transglut_core. 1 hit.
    PF00868. Transglut_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000459. TGM_EBP42. 1 hit.
    SMARTi SM00460. TGc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49309. SSF49309. 2 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS00547. TRANSGLUTAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of mouse erythrocyte protein 4.2: a membrane protein with strong homology with the transglutaminase supergene family."
      Rybicki A.C., Schwartz R.S., Qiu J.J.-H., Gilman J.G.
      Mamm. Genome 5:438-445(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
      Tissue: Reticulocyte.
    2. "cDNA sequence, gene sequence, and properties of murine pallidin (band 4.2), the protein implicated in the murine pallid mutation."
      Korsgren C., Cohen C.M.
      Genomics 21:478-485(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: BALB/c and C57BL/6J.
      Tissue: Liver and Reticulocyte.
    3. "Murine erythrocyte protein 4.2 gene: similarity and differences in structure and expression from its human counterpart."
      Karacay B.B.K., Enzhong X.E.X., Chang L.-S.L.S.
      Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    4. "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: Spleen.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.

    Entry informationi

    Entry nameiEPB42_MOUSE
    AccessioniPrimary (citable) accession number: P49222
    Secondary accession number(s): Q3UP33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 130 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The substitution of an Ala for a Cys in the active site may be responsible for the lack of transglutaminase activity of band 4.2.

    Caution

    Was originally thought to be pallidin.1 Publication

    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