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 03-AUG-2022, entry version 177.
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: Probably plays an important role in the regulation of
CC erythrocyte shape and mechanical properties.
CC -!- SUBUNIT: Oligomer. Interacts with the cytoplasmic domain of SLC4A1/band
CC 3 anion transport protein.
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; P49222; -.
DR PeptideAtlas; P49222; -.
DR PRIDE; P49222; -.
DR ProteomicsDB; 275625; -.
DR Antibodypedia; 11125; 109 antibodies from 18 providers.
DR DNASU; 13828; -.
DR Ensembl; ENSMUST00000102490; ENSMUSP00000099548; ENSMUSG00000023216.
DR GeneID; 13828; -.
DR KEGG; mmu:13828; -.
DR UCSC; uc008lxi.1; mouse.
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; 297055at2759; -.
DR PhylomeDB; P49222; -.
DR TreeFam; TF324278; -.
DR BioGRID-ORCS; 13828; 0 hits in 39 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 78 other tissues.
DR ExpressionAtlas; P49222; baseline and differential.
DR Genevisible; P49222; MM.
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:ion homeostasis; IMP:MGI.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:MGI.
DR GO; GO:0018149; P:peptide cross-linking; IBA:GO_Central.
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; -; 3.
DR Gene3D; 3.90.260.10; -; 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 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; SSF49309; SSF49309; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
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
