ID   EPB42_BOVIN             Reviewed;         687 AA.
AC   O46510; O46509;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Protein 4.2 {ECO:0000305};
DE            Short=P4.2 {ECO:0000305};
DE   AltName: Full=Erythrocyte membrane protein band 4.2 {ECO:0000250|UniProtKB:P16452};
DE            Short=Erythrocyte protein 4.2 {ECO:0000250|UniProtKB:P16452};
GN   Name=EPB42 {ECO:0000250|UniProtKB:P16452};
GN   Synonyms=BEP42 {ECO:0000312|EMBL:AAC48854.1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PRO-599; MET-601 AND VAL-627.
RC   STRAIN=Japanese black;
RX   PubMed=9576866; DOI=10.1042/bj3320183;
RA   Matsumoto M., Inaba M., Ono K.;
RT   "Molecular basis of bovine red-cell protein 4.2 polymorphism in Japanese
RT   black cattle.";
RL   Biochem. J. 332:183-187(1998).
CC   -!- FUNCTION: Probably plays an important role in the regulation of
CC       erythrocyte shape and mechanical properties. {ECO:0000250}.
CC   -!- SUBUNIT: Oligomer. Interacts with the cytoplasmic domain of SLC4A1/band
CC       3 anion transport protein. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm,
CC       cytoskeleton {ECO:0000250}. Note=Cytoplasmic surface of erythrocyte
CC       membranes. {ECO:0000250}.
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}.
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DR   EMBL; AF030029; AAC48854.1; -; mRNA.
DR   EMBL; AF030030; AAC48855.1; -; mRNA.
DR   RefSeq; NP_776737.1; NM_174312.2.
DR   AlphaFoldDB; O46510; -.
DR   SMR; O46510; -.
DR   STRING; 9913.ENSBTAP00000035838; -.
DR   PRIDE; O46510; -.
DR   Ensembl; ENSBTAT00000035972; ENSBTAP00000035838; ENSBTAG00000011439.
DR   GeneID; 281754; -.
DR   KEGG; bta:281754; -.
DR   CTD; 2038; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011439; -.
DR   VGNC; VGNC:28526; EPB42.
DR   GeneTree; ENSGT01050000244866; -.
DR   InParanoid; O46510; -.
DR   OMA; NPWGRED; -.
DR   OrthoDB; 297055at2759; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000011439; Expressed in oocyte and 17 other tissues.
DR   ExpressionAtlas; O46510; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR   GO; GO:0018149; P:peptide cross-linking; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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   2: Evidence at transcript 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..687
FT                   /note="Protein 4.2"
FT                   /id="PRO_0000213719"
FT   REGION          31..39
FT                   /note="Band 3 binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16452"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
FT   VARIANT         599
FT                   /note="T -> P"
FT                   /evidence="ECO:0000269|PubMed:9576866"
FT   VARIANT         601
FT                   /note="I -> M"
FT                   /evidence="ECO:0000269|PubMed:9576866"
FT   VARIANT         627
FT                   /note="I -> V"
FT                   /evidence="ECO:0000269|PubMed:9576866"
SQ   SEQUENCE   687 AA;  76617 MW;  AB0348C2942E1E58 CRC64;
     MGQGLGIKSC DFQAARNNAE HHTNDISSQR LFVRRGQPFT ISLHFQAPVH TFLRALKKVA
     LIAQTGKQPS KANGTQATFS VSSLGDRKWW SAMVEERDDQ SWTISVTTPA DAIIGHYSLL
     LQISGRKQCL GQFTLLFNPW NREDAVFLGN EAQRKEYLLN QNGLIFLGTA DCIQAEPWDF
     GQLEEDVIDL GLSLLTVDNQ VEKWGNPVHV ARVLGALLHI LKEKSVLPTA KIQTTEERAL
     LNKRRGSAPI LRQWVTGHGR PVYEGQAWVL AAVACTVLRG LGIPARVVTT FTSAQGTGGD
     LLVNEYYNEE GLQNGEDNRG RAWIFQTSTE CWMARPDLLE VYDGWQILYP SALKGGEVLE
     ACDLVPVRAV KEGIVWLTPA ASDIFASINA SCVVWKCGED GTLELTDSNT KYFGNNISTK
     NVDCDCHEDI TQNYKYPEGS SQEKMVLEKV QKYRMKHKND GIYPPCCETD DPLHLFLKAP
     SSLALGKNVE ISVNLLNPTD QEKEVQLAIG LQAMYYNGVL AAKLWRKNFV LILSANSAKK
     ISTSLFNSNF EQSLPENSFL RLTAMATHSS LPCFAQQDIA IRRPHLAIEM PETAEQHQTL
     IALVSIHNPL DVPLEDCVIS IFGKGLIHRE KSYRVNSVQP RNTLRTQLKF VPMKVGCQRL
     TVEMDCNMFQ NLTNFRTVMV VAPKSPA