ID GCA2_BOVIN STANDARD; PRT; 203 AA. AC P51177; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE GUANYLATE CYCLASE ACTIVATING PROTEIN 2 (GCAP 2) (GUANYLATE CYCLASE DE ACTIVATOR 1B) (RETINAL GUANYLYL CYCLASE ACTIVATOR PROTEIN P24). GN GUCA1B OR GCAP2 OR GCAP-2. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=RETINA; RX MEDLINE=96027628; PubMed=7559656; RA Dizhoor A.M., Olshevskaya E.V., Henzel W.J., Wong S.C., Stults J.T., RA Ankoudinova I., Hurley J.B.; RT "Cloning, sequencing, and expression of a 24-kDa Ca(2+)-binding RT protein activating photoreceptor guanylyl cyclase."; RL J. Biol. Chem. 270:25200-25206(1995). RN [2] RP SEQUENCE FROM N.A., AND SEQUENCE OF 50-80. RC TISSUE=RETINA; RX MEDLINE=95394975; PubMed=7665624; RA Gorczyca W.A., Polans A.S., Surgucheva I.G., Subbaraya I., Baehr W., RA Palczewski K.; RT "Guanylyl cyclase activating protein. A calcium-sensitive regulator of RT phototransduction."; RL J. Biol. Chem. 270:22029-22036(1995). CC -!- FUNCTION: STIMULATES SYNTHESIS OF CGMP IN PHOTORECEPTORS. THOUGHT CC TO MEDIATE CA(2+)-SENSITIVE REGULATION OF GUANYLYL CYCLASE (GC), A CC KEY EVENT IN RECOVERY OF THE DARK STATE OF ROD PHOTORECEPTORS CC FOLLOWING LIGHT EXPOSURE. CC -!- SUBCELLULAR LOCATION: MEMBRANES OF OUTER SEGMENT. CC -!- TISSUE SPECIFICITY: RETINA. APPEARS TO BE MORE ABUNDANT IN RODS. CC -!- PTM: THE N-TERMINUS IS BLOCKED. CC -!- SIMILARITY: CONTAINS 4 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; U32856; AAC48478.1; -. DR EMBL; L43001; AAA83214.1; -. DR HSSP; P02593; 1CMF. DR INTERPRO; IPR002048; -. DR PFAM; PF00036; efhand; 3. DR PROSITE; PS00018; EF_HAND; 3. KW Calcium-binding; Repeat; Vision; Myristate. FT INIT_MET 0 0 POTENTIAL. FT LIPID 1 1 MYRISTATE (POTENTIAL). FT DOMAIN 32 43 ANCESTRAL CALCIUM SITE 1 (POTENTIAL). FT CA_BIND 68 79 SITE 2 (POTENTIAL). FT CA_BIND 104 115 SITE 3 (POTENTIAL). FT CA_BIND 157 168 SITE 4 (POTENTIAL). SQ SEQUENCE 203 AA; 23597 MW; 3C2B13C47126A9D5 CRC64; GQQFSWEEAE ENGAVGAADA AQLQEWYKKF LEECPSGTLF MHEFKRFFKV PDNEEATQYV EAMFRAFDTN GDNTIDFLEY VAALNLVLRG TLEHKLKWTF KIYDKDRNGC IDRQELLDIV ESIYKLKKAC SVEVEAEQQG KLLTPEEVVD RIFLLVDENG DGQLSLNEFV EGARRDKWVM KMLQMDLNPS SWISQQRRKS AMF //