ID 42_HUMAN STANDARD; PRT; 690 AA. AC P16452; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE ERYTHROCYTE MEMBRANE PROTEIN BAND 4.2 (P4.2) (PALLIDIN). GN EPB42 OR E42P. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (LONG ISOFORM). RC TISSUE=RETICULOCYTES; RX MEDLINE=91271288; PubMed=2052563; RA Korsgren C., Cohen C.M.; RT "Organization of the gene for human erythrocyte membrane protein 4.2: RT structural similarities with the gene for the a subunit of factor RT XIII."; RL Proc. Natl. Acad. Sci. U.S.A. 88:4840-4844(1991). RN [2] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE (SHORT ISOFORM). RC TISSUE=RETICULOCYTES; RX MEDLINE=90138879; PubMed=2300550; RA Korsgren C., Lawler J., Lambert S., Speicher D., Cohen C.M.; RT "Complete amino acid sequence and homologies of human erythrocyte RT membrane protein band 4.2."; RL Proc. Natl. Acad. Sci. U.S.A. 87:613-617(1990). RN [3] RP SEQUENCE FROM N.A. (SHORT AND LONG ISOFORMS). RC TISSUE=RETICULOCYTES; RX MEDLINE=90138995; PubMed=1689063; RA Sung L.A., Chien S., Chang L.-S., Lambert K., Bliss S.A., RA Bouhassira E.E., Nagel R.L., Schwartz R.S., Rybicki A.C.; RT "Molecular cloning of human protein 4.2: a major component of the RT erythrocyte membrane."; RL Proc. Natl. Acad. Sci. U.S.A. 87:955-959(1990). RN [4] RP MYRISTOYLATION. RX MEDLINE=92184834; PubMed=1544941; RA Risinger M.A., Dotimas E.M., Cohen C.M.; RT "Human erythrocyte protein 4.2, a high copy number membrane protein, RT is N-myristylated."; RL J. Biol. Chem. 267:5680-5685(1992). RN [5] RP PHOSPHORYLATION OF SER-247. RX MEDLINE=93271204; PubMed=8499466; RA Dotimas E., Speicher D.W., Guptaroy B., Cohen C.M.; RT "Structural domain mapping and phosphorylation of human erythrocyte RT pallidin (band 4.2)."; RL Biochim. Biophys. Acta 1148:19-29(1993). RN [6] RP VARIANT HS NIPPON. RX MEDLINE=92216098; PubMed=1558976; RA Bouhassira E.E., Schwartz R.S., Yawata Y., Ata K., Kanzaki A., RA Qiu J.J., Nagel R.L., Rybicki A.C.; RT "An alanine-to-threonine substitution in protein 4.2 cDNA is RT associated with a Japanese form of hereditary hemolytic anemia RT (protein 4.2NIPPON)."; RL Blood 79:1846-1854(1992). RN [7] RP VARIANT HS NIPPON. RX MEDLINE=95118828; PubMed=7819064; RA Takaoka Y., Ideguchi H., Matsuda M., Sakamoto N., Takeuchi T., RA Fukumaki Y.; RT "A novel mutation in the erythrocyte protein 4.2 gene of Japanese RT patients with hereditary spherocytosis (protein 4.2 Fukuoka)."; RL Br. J. Haematol. 88:527-533(1994). CC -!- FUNCTION: BAND 4.2 PROBABLY PLAYS AN IMPORTANT ROLE IN THE CC REGULATION OF ERYTHROCYTE SHAPE AND MECHANICAL PROPERTIES. CC THE MAJOR MEMBRANE BINDING FOR BAND 4.2 IS THE CYTOPLASMIC CC DOMAIN OF THE ERYTHROCYTE ANION TRANSPORTER, BAND 3. CC -!- SUBUNIT: OLIGOMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC SURFACE OF ERYTHROCYTE CC MEMBRANES. CC -!- ALTERNATIVE PRODUCTS: TWO ISOFORMS ARE PRODUCED BY ALTERNATIVE CC SPLICING. THE SHORTER FORM IS MORE ABUNDANT. CC -!- PTM: BOTH CAMP-DEPENDENT KINASE (CAPK) AND ANOTHER KINASE PRESENT CC IN THE RED-BLOOD CELLS SEEM TO BE ABLE TO PHOSPHORYLATE EPB42. CC -!- DISEASE: INDIVIDUALS WHOSE ERYTHROCYTES LACK OR ARE DEFICIENT IN CC BAND 4.2 HAVE HEMOLYTIC ANEMIA ASSOCIATED WITH SPHEROCYTIC (HS) OR CC ELLIPTOCYTIC ERYTHROCYTES. ABSENCE OF BAND 4.2 ASSOCIATED WITH CC SPUR OR TARGET ERYTHROCYTES HAS ALSO BEEN REPORTED. CC -!- MISCELLANEOUS: THE SUBSTITUTION IN BAND 4.2 OF AN ALA FOR A CYS IN CC THE ACTIVE SITE MAY BE RESPONSIBLE FOR THE LACK OF CC TRANSGLUTAMINASE ACTIVITY OF BAND 4.2. CC -!- SIMILARITY: BELONGS TO THE TRANSGLUTAMINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M60298; AAA74589.1; -. DR EMBL; L06519; AAA52385.1; -. DR EMBL; L06447; AAA52385.1; JOINED. DR EMBL; L06448; AAA52385.1; JOINED. DR EMBL; L06449; AAA52385.1; JOINED. DR EMBL; L06450; AAA52385.1; JOINED. DR EMBL; L06511; AAA52385.1; JOINED. DR EMBL; L06512; AAA52385.1; JOINED. DR EMBL; L06513; AAA52385.1; JOINED. DR EMBL; L06515; AAA52385.1; JOINED. DR EMBL; L06516; AAA52385.1; JOINED. DR EMBL; L06517; AAA52385.1; JOINED. DR EMBL; L06518; AAA52385.1; JOINED. DR EMBL; M29399; AAA35798.1; -. DR EMBL; M30646; AAA36402.1; -. DR EMBL; M30647; AAA36401.1; -. DR PIR; A34865; A34865. DR PIR; A34883; A34883. DR MIM; 177070; -. DR INTERPRO; IPR001102; -. DR INTERPRO; IPR002931; -. DR PFAM; PF01841; Transglut_core; 1. DR PFAM; PF00927; Transglutamin_C; 1. DR PFAM; PF00868; Transglutamin_N; 1. DR PROSITE; PS00547; TRANSGLUTAMINASES; 1. KW Structural protein; Erythrocyte maturation; Myristate; KW Phosphorylation; Alternative splicing; Disease mutation. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE. FT BINDING 30 38 TO BAND 3 (BY SIMILARITY). FT MOD_RES 247 247 PHOSPHORYLATION (BY CAPK) (PROBABLE). FT VARSPLIC 2 2 Q -> QGEPSQRSTGLAGLYAAPAASPVFIKGSGMD (IN FT LONG ISOFORM). FT VARIANT 111 111 A -> T (IN HS; NIPPON). FT /FTID=VAR_007482. FT CONFLICT 334 339 TRPALP -> KRGLPC (IN REF. 3). FT CONFLICT 349 349 D -> H (IN REF. 3). FT CONFLICT 375 375 V -> L (IN REF. 3). SQ SEQUENCE 690 AA; 76841 MW; C6E605E69A0A7A8B CRC64; GQALGIKSCD FQAARNNEEH HTKALSSRRL FVRRGQPFTI ILYFRAPVRA FLPALKKVAL TAQTGEQPSK INRTQATFPI SSLGDRKWWS AVVEERDAQS WTISVTTPAD AVIGHYSLLL QVSGRKQLLL GQFTLLFNPW NREDAVFLKN EAQRMEYLLN QNGLIYLGTA DCIQAESWDF GQFEGDVIDL SLRLLSKDKQ VEKWSQPVHV ARVLGALLHF LKEQRVLPTP QTQATQEGAL LNKRRGSVPI LRQWLTGRGR PVYDGQAWVL AAVACTVLRC LGIPARVVTT FASAQGTGGR LLIDEYYNEE GLQNGEGQRG RIWIFQTSTE CWMTRPALPQ GYDGWQILDP SAPNGGGVLG SCDLVPVRAV KEGTVGLTPA VSDLFAAINA SCVVWKCCED GTLELTDSNT KYVGNNISTK GVGSDRCEDI TQNYKYPEGS LQEKEVLERV EKEKMEREKD NGIRPPSLET ASPLYLLLKA PSSLPLRGDA QISVTLVNHS EQEKAVQLAI GVQAVHYNGV LAAKLWRKKL HLTLSANLEK IITIGLFFSN FERNPPENTF LRLTAMATHS ESNLSCFAQE DIAICRPHLA IKMPEKAEQY QPLTASVSLQ NSLDAPMEDC VISILGRGLI HRERSYRFRS VWPENTMCAK FQFTPTHVGL QRLTVEVDCN MFQNLTNYKS VTVVAPELSA //