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P49222

- EPB42_MOUSE

UniProt

P49222 - EPB42_MOUSE

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

BgeeiP49222.
CleanExiMM_EPB4.2.
ExpressionAtlasiP49222. baseline and differential.
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.
GeneTreeiENSGT00760000119108.
HOGENOMiHOG000231695.
HOVERGENiHBG106048.
InParanoidiP49222.
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

        10         20         30         40         50
MGQALSIKSC DFHAAENNEE HYTKAISSQH LTLRRGQSFT ITLNFRAPTH
60 70 80 90 100
TFLSALKKVA LIAQTGEQPS KINKTQAIFP ISSLGDQKGW SAAVEERDAQ
110 120 130 140 150
HWTVSVTTPV DAVIGHYSLL LQVSGKKQYP LGQFTLLFNP WNRDDAVFLQ
160 170 180 190 200
NEAERTEYVL NQNGFIYLGT ADCIQEEPWD FGQFEKDVMD LSLKLLSMDK
210 220 230 240 250
QVKDWNQPAH VARVVGALLH ALKKKSVLPI SQTQAAQEGA LLYKRRGSVP
260 270 280 290 300
ILRQWLTGQG RAVYETQAWV SAAVACTVLR CLGIPARVVT TFDSAQGTVG
310 320 330 340 350
SLLVDEYYNE EGLQNGEGQR GHIWVFQTSV ECWMNRPDLS QGYGGWQILH
360 370 380 390 400
PRAPNGAGVL GSCSLVPVRA VKEGELQLDP AVPELFAAVN ASCVVWKCCE
410 420 430 440 450
DGKLELTNSN RKDVGNCIST KVVGSDRCED ITQNYKYPAG SLQEKEVLEK
460 470 480 490 500
VQKERLKLGK DNGMCPPSCE PWDPLHMFFE ASSSIPLSGD GQLSVTLINP
510 520 530 540 550
TDEEKKVHLV IGAQALYYNG VLAAGLWSKK QLFMLKPNQV MRLSTNLSFS
560 570 580 590 600
CFEQTPPENS FLRVTAMARY SHTSLSCFAQ ENMAIGKPDL IIEMPKRAAQ
610 620 630 640 650
YRPLTVSVRM HNSLEAPMQN CIISIFGRGL IHREKRYGLG SLWPGSSLHT
660 670 680 690
QFQFTPTHLG LQRLTVEVDC DMFQNLTGYR SVLVVAPEVS V
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 ENSGT00760000119108.
HOGENOMi HOG000231695.
HOVERGENi HBG106048.
InParanoidi P49222.
OMAi SCFAQED.
OrthoDBi EOG7Z0JVS.
TreeFami TF324278.

Miscellaneous databases

NextBioi 284632.
PROi P49222.
SOURCEi Search...

Gene expression databases

Bgeei P49222.
CleanExi MM_EPB4.2.
ExpressionAtlasi P49222. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 131 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