ID   42_MOUSE       STANDARD;      PRT;   690 AA.
AC   P49222;
DT   01-FEB-1996 (Rel. 33, Created)
DT   01-FEB-1996 (Rel. 33, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   ERYTHROCYTE MEMBRANE PROTEIN BAND 4.2 (P4.2) (PALLIDIN).
GN   EPB42 OR EPB4.2 OR PA.
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=C57BL/6J; TISSUE=RETICULOCYTES;
RX   MEDLINE=95003352; PubMed=7919657;
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
RT   protein with strong homology with the transglutaminase supergene
RT   family.";
RL   Mamm. Genome 5:438-445(1994).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=C57BL/6J, AND BALB/C; TISSUE=RETICULOCYTES, AND LIVER;
RX   MEDLINE=95048323; PubMed=7959722;
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).
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   -!- DISEASE: A DEFECT IN EPB42, KNOWN AS PALLID, AFFECTS THE FORMATION
CC       OR FUNCTION OF INTRACELLULAR STORAGE GRANULES IN MELANOCYTES AND
CC       PLATELETS AND LYSOSOMES IN KIDNEY. PALLID MICE HAVE A PROLONGED
CC       BLEEDING TIME OWING TO THE INABILITY OF IMMATURE PLATELET DENSE
CC       GRANULES TO ACCUMULATE NORMAL AMOUNTS OF ATP, ADP, AND SEROTONIN.
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   --------------------------------------------------------------------------
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DR   EMBL; U03487; AAA62275.1; -.
DR   EMBL; U04055; AAA67916.1; -.
DR   EMBL; U04056; AAA67917.1; -.
DR   EMBL; L35933; AAA39875.1; -.
DR   MGD; MGI:95402; Epb4.2.
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.
FT   INIT_MET      0      0       BY SIMILARITY.
FT   LIPID         1      1       MYRISTATE (BY SIMILARITY).
FT   BINDING      30     38       TO BAND 3 (BY SIMILARITY).
FT   MOD_RES     247    247       PHOSPHORYLATION (BY SIMILARITY).
FT   CONFLICT     21     21       Y -> H (IN AAA67917).
FT   CONFLICT    223    223       K -> N (IN AAA67917).
FT   CONFLICT    397    397       C -> S (IN AAA67917).
FT   CONFLICT    449    449       K -> R (IN AAA67917).
FT   CONFLICT    527    527       S -> R (IN AAA67917).
FT   CONFLICT    620    620       S -> C (IN REF. 2).
SQ   SEQUENCE   690 AA;  76608 MW;  3F6BCEF23DD385A6 CRC64;
     GQALSIKSCD FHAAENNEEH YTKAISSQHL TLRRGQSFTI TLNFRAPTHT FLSALKKVAL
     IAQTGEQPSK INKTQAIFPI SSLGDQKGWS AAVEERDAQH WTVSVTTPVD AVIGHYSLLL
     QVSGKKQYPL GQFTLLFNPW NRDDAVFLQN EAERTEYVLN QNGFIYLGTA DCIQEEPWDF
     GQFEKDVMDL SLKLLSMDKQ VKDWNQPAHV ARVVGALLHA LKKKSVLPIS QTQAAQEGAL
     LYKRRGSVPI LRQWLTGQGR AVYETQAWVS AAVACTVLRC LGIPARVVTT FDSAQGTVGS
     LLVDEYYNEE GLQNGEGQRG HIWVFQTSVE CWMNRPDLSQ GYGGWQILHP RAPNGAGVLG
     SCSLVPVRAV KEGELQLDPA VPELFAAVNA SCVVWKCCED GKLELTNSNR KDVGNCISTK
     VVGSDRCEDI TQNYKYPAGS LQEKEVLEKV QKERLKLGKD NGMCPPSCEP WDPLHMFFEA
     SSSIPLSGDG QLSVTLINPT DEEKKVHLVI GAQALYYNGV LAAGLWSKKQ LFMLKPNQVM
     RLSTNLSFSC FEQTPPENSF LRVTAMARYS HTSLSCFAQE NMAIGKPDLI IEMPKRAAQY
     RPLTVSVRMH NSLEAPMQNS IISIFGRGLI HREKRYGLGS LWPGSSLHTQ FQFTPTHLGL
     QRLTVEVDCD MFQNLTGYRS VLVVAPEVSV
//