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Database: UniProt
Entry: EPB42_MOUSE
LinkDB: EPB42_MOUSE
Original site: EPB42_MOUSE 
ID   EPB42_MOUSE             Reviewed;         691 AA.
AC   P49222; Q3UP33;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   24-JAN-2024, entry version 185.
DE   RecName: Full=Protein 4.2 {ECO:0000305};
DE            Short=P4.2 {ECO:0000305};
DE   AltName: Full=Erythrocyte membrane protein band 4.2 {ECO:0000312|MGI:MGI:95402};
DE            Short=Erythrocyte protein 4.2 {ECO:0000303|PubMed:7919657};
GN   Name=Epb42 {ECO:0000312|MGI:MGI:95402};
GN   Synonyms=Epb4.2 {ECO:0000312|MGI:MGI:95402};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Reticulocyte;
RX   PubMed=7919657; DOI=10.1007/bf00357005;
RA   Rybicki A.C., Schwartz R.S., Qiu J.J.-H., Gilman J.G.;
RT   "Molecular cloning of mouse erythrocyte protein 4.2: a membrane protein
RT   with strong homology with the transglutaminase supergene family.";
RL   Mamm. Genome 5:438-445(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Liver, and Reticulocyte;
RX   PubMed=7959722; DOI=10.1006/geno.1994.1304;
RA   Korsgren C., Cohen C.M.;
RT   "cDNA sequence, gene sequence, and properties of murine pallidin (band
RT   4.2), the protein implicated in the murine pallid mutation.";
RL   Genomics 21:478-485(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Blood;
RA   Karacay B.B.K., Enzhong X.E.X., Chang L.-S.L.S.;
RT   "Murine erythrocyte protein 4.2 gene: similarity and differences in
RT   structure and expression from its human counterpart.";
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-570, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex
CC       involved in the stability and shape of the erythrocyte membrane.
CC       {ECO:0000250|UniProtKB:P16452}.
CC   -!- SUBUNIT: Component of the ankyrin-1 complex in the erythrocyte,
CC       composed of ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB and AQP1.
CC       Interacts with SLC4A1 (via the cytoplasmic domain); this interaction is
CC       mediated by the SLC4A1 Band 3-I dimer. Interacts with ANK1 (via ANK 1-
CC       13 repeats). Interacts with AQP1 (via the C-terminal).
CC       {ECO:0000250|UniProtKB:P16452}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side.
CC       Cytoplasm, cytoskeleton. Note=Cytoplasmic surface of erythrocyte
CC       membranes.
CC   -!- MISCELLANEOUS: The substitution of an Ala for a Cys in the active site
CC       may be responsible for the lack of transglutaminase activity of band
CC       4.2.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be pallidin.
CC       {ECO:0000305|PubMed:7959722}.
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DR   EMBL; U03487; AAA62275.1; -; mRNA.
DR   EMBL; U04055; AAA67916.1; -; mRNA.
DR   EMBL; U04056; AAA67917.1; -; Genomic_DNA.
DR   EMBL; L35933; AAA39875.1; -; mRNA.
DR   EMBL; AK143841; BAE25564.1; -; mRNA.
DR   EMBL; AL844548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS16631.1; -.
DR   PIR; A54741; A54741.
DR   RefSeq; NP_038541.1; NM_013513.3.
DR   AlphaFoldDB; P49222; -.
DR   SMR; P49222; -.
DR   BioGRID; 199463; 1.
DR   STRING; 10090.ENSMUSP00000099548; -.
DR   iPTMnet; P49222; -.
DR   PhosphoSitePlus; P49222; -.
DR   jPOST; P49222; -.
DR   MaxQB; P49222; -.
DR   PaxDb; 10090-ENSMUSP00000099548; -.
DR   PeptideAtlas; P49222; -.
DR   ProteomicsDB; 275625; -.
DR   Antibodypedia; 11125; 131 antibodies from 19 providers.
DR   DNASU; 13828; -.
DR   Ensembl; ENSMUST00000102490.10; ENSMUSP00000099548.4; ENSMUSG00000023216.14.
DR   GeneID; 13828; -.
DR   KEGG; mmu:13828; -.
DR   UCSC; uc008lxi.1; mouse.
DR   AGR; MGI:95402; -.
DR   CTD; 2038; -.
DR   MGI; MGI:95402; Epb42.
DR   VEuPathDB; HostDB:ENSMUSG00000023216; -.
DR   eggNOG; ENOG502R9T9; Eukaryota.
DR   GeneTree; ENSGT01050000244866; -.
DR   HOGENOM; CLU_013435_3_0_1; -.
DR   InParanoid; P49222; -.
DR   OMA; NPWGRED; -.
DR   OrthoDB; 5344745at2759; -.
DR   PhylomeDB; P49222; -.
DR   TreeFam; TF324278; -.
DR   BioGRID-ORCS; 13828; 0 hits in 44 CRISPR screens.
DR   PRO; PR:P49222; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P49222; Protein.
DR   Bgee; ENSMUSG00000023216; Expressed in fetal liver hematopoietic progenitor cell and 80 other cell types or tissues.
DR   ExpressionAtlas; P49222; baseline and differential.
DR   Genevisible; P49222; MM.
DR   GO; GO:0170014; C:ankyrin-1 complex; ISS:UniProtKB.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR   GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR   GO; GO:0020027; P:hemoglobin metabolic process; IMP:MGI.
DR   GO; GO:0050801; P:monoatomic ion homeostasis; IMP:MGI.
DR   GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; IMP:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0048536; P:spleen development; IMP:MGI.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   InterPro; IPR036985; Transglutaminase-like_sf.
DR   InterPro; IPR023608; Transglutaminase_animal.
DR   InterPro; IPR013808; Transglutaminase_AS.
DR   InterPro; IPR008958; Transglutaminase_C.
DR   InterPro; IPR036238; Transglutaminase_C_sf.
DR   InterPro; IPR001102; Transglutaminase_N.
DR   PANTHER; PTHR11590:SF44; PROTEIN 4.2; 1.
DR   PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR   Pfam; PF00927; Transglut_C; 2.
DR   Pfam; PF01841; Transglut_core; 1.
DR   Pfam; PF00868; Transglut_N; 1.
DR   PIRSF; PIRSF000459; TGM_EBP42; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell shape; Cytoplasm; Cytoskeleton; Erythrocyte maturation;
KW   Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..691
FT                   /note="Protein 4.2"
FT                   /id="PRO_0000213721"
FT   REGION          31..39
FT                   /note="Band 3 binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16452"
FT   MOD_RES         570
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        22
FT                   /note="Y -> H (in Ref. 2; AAA67917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224
FT                   /note="K -> N (in Ref. 2; AAA67917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        398
FT                   /note="C -> S (in Ref. 2; AAA67917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        450
FT                   /note="K -> R (in Ref. 2; AAA67917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        528
FT                   /note="S -> R (in Ref. 2; AAA67917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        621
FT                   /note="C -> S (in Ref. 1; AAA62275)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   691 AA;  76756 MW;  433E1623971D60C3 CRC64;
     MGQALSIKSC DFHAAENNEE HYTKAISSQH LTLRRGQSFT ITLNFRAPTH TFLSALKKVA
     LIAQTGEQPS KINKTQAIFP ISSLGDQKGW SAAVEERDAQ HWTVSVTTPV DAVIGHYSLL
     LQVSGKKQYP LGQFTLLFNP WNRDDAVFLQ NEAERTEYVL NQNGFIYLGT ADCIQEEPWD
     FGQFEKDVMD LSLKLLSMDK QVKDWNQPAH VARVVGALLH ALKKKSVLPI SQTQAAQEGA
     LLYKRRGSVP ILRQWLTGQG RAVYETQAWV SAAVACTVLR CLGIPARVVT TFDSAQGTVG
     SLLVDEYYNE EGLQNGEGQR GHIWVFQTSV ECWMNRPDLS QGYGGWQILH PRAPNGAGVL
     GSCSLVPVRA VKEGELQLDP AVPELFAAVN ASCVVWKCCE DGKLELTNSN RKDVGNCIST
     KVVGSDRCED ITQNYKYPAG SLQEKEVLEK VQKERLKLGK DNGMCPPSCE PWDPLHMFFE
     ASSSIPLSGD GQLSVTLINP TDEEKKVHLV IGAQALYYNG VLAAGLWSKK QLFMLKPNQV
     MRLSTNLSFS CFEQTPPENS FLRVTAMARY SHTSLSCFAQ ENMAIGKPDL IIEMPKRAAQ
     YRPLTVSVRM HNSLEAPMQN CIISIFGRGL IHREKRYGLG SLWPGSSLHT QFQFTPTHLG
     LQRLTVEVDC DMFQNLTGYR SVLVVAPEVS V
//
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