ID CA22_HUMAN STANDARD; PRT; 194 AA. AC Q99653; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE CALCIUM-BINDING PROTEIN P22 (CALCIUM-BINDING PROTEIN CHP) (CALCINEURIN DE B HOMOLOGOUS PROTEIN). 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. RC TISSUE=B-CELL; RX MEDLINE=97057295; PubMed=8901634; RA Lin X., Barber D.L.; RT "A calcineurin homologous protein inhibits GTPase-stimulated Na-H RT exchange."; RL Proc. Natl. Acad. Sci. U.S.A. 93:12631-12636(1996). CC -!- FUNCTION: REQUIRED FOR CONSTITUTIVE MEMBRANE TRAFFIC (BY CC SIMILARITY). INHIBITS GTPASE-STIMULATED NA-H EXCHANGE. CC SPECIFICALLY BINDS TO THE SODIUM/HYDROGEN EXCHANGER 1 (NHE1) AT A CC DOMAIN THAT IS CRITICAL FOR GROWTH FACTOR STIMULATION OF EXCHANGE CC ACTIVITY. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: UBIQUITOUSLY EXPRESSED. HAS BEEN FOUND IN CC FETAL EYE, LUNG, LIVER, MUSCLE, HEART, KIDNEY, THYMUS AND SPLEEN. CC -!- PTM: BOTH N-MYRISTOYLATION AND CALCIUM-MEDIATED CONFORMATIONAL CC CHANGES ARE ESSENTIAL FOR ITS FUNCTION IN EXOCYTIC TRAFFIC CC (BY SIMILARITY). CC -!- PTM: PHOSPHORYLATED IN VIVO. DECREASE IN ITS PHOSPHORYLATION IS CC ASSOCIATED WITH AN INCREASE IN EXCHANGE ACTIVITY. THE CC PHOSPHORYLATION STATE MAY REGULATE THE BINDING TO NHE1. CC -!- SIMILARITY: CONTAINS 2 EF-HAND CALCIUM-BINDING DOMAINS. 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; U61538; AAB37770.1; -. DR HSSP; P06705; 1AUI. DR INTERPRO; IPR002048; -. DR PFAM; PF00036; efhand; 2. DR PROSITE; PS00018; EF_HAND; FALSE_NEG. KW Calcium-binding; Repeat; Myristate; Phosphorylation. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT DOMAIN 38 49 ANCESTRAL CALCIUM SITE 1 (POTENTIAL). FT DOMAIN 70 81 ANCESTRAL CALCIUM SITE 2 (POTENTIAL). FT CA_BIND 122 133 SITE 3 (BY SIMILARITY). FT CA_BIND 163 174 SITE 4 (BY SIMILARITY). SQ SEQUENCE 194 AA; 22325 MW; 17DDEE5F03C88380 CRC64; GSRASTLLRD EELEEIKKET GFSHSQITRL YSRFTSLDKG ENGTLSREDF QRIPELAINP LGDRIINAFF PEGEDQVNFR GFMRTLAHFR PIEDNEKSKD VNGPEPLNSR SNKLHFAFRL YDLDKDEKIS RDELLQVLRM MVGVNISDEQ LGSIADRTIQ EADQDGDSAI SFTEFVKVLE KVDVEQKMSI RFLH //