SMOD_LITCT
ID SMOD_LITCT Reviewed; 202 AA.
AC P31227;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=S-modulin;
DE AltName: Full=Sensitivity-modulating protein;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=8392055; DOI=10.1016/s0021-9258(18)82369-9;
RA Kawamura S., Hisatomi O., Kayada S., Tokunaga F., Kuo C.-H.;
RT "Recoverin has S-modulin activity in frog rods.";
RL J. Biol. Chem. 268:14579-14582(1993).
RN [2]
RP PROTEIN SEQUENCE OF 22-28; 47-55; 63-97; 131-150; 154-162; 167-177 AND
RP 180-192.
RC TISSUE=Retina;
RX PubMed=1321610; DOI=10.1016/s0006-291x(05)80823-x;
RA Kawamura S., Takamatsu K., Kitamura K.;
RT "Purification and characterization of S-modulin, a calcium-dependent
RT regulator on cGMP phosphodiesterase in frog rod photoreceptors.";
RL Biochem. Biophys. Res. Commun. 186:411-417(1992).
CC -!- FUNCTION: Calcium-dependent regulator of light sensitivity of cGMP
CC phosphodiesterase in rod outer segments. Control rhodopsin
CC phosphorylation in a Ca(2+)-dependent manner.
CC -!- SUBCELLULAR LOCATION: Note=The binding target of the Ca(2+)/S-modulin
CC complex is possibly ROS membrane lipid(s).
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; D83641; BAA19728.1; -; mRNA.
DR PIR; JC1107; JC1107.
DR PIR; T10531; T10531.
DR AlphaFoldDB; P31227; -.
DR SMR; P31227; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028846; Recoverin.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Lipoprotein; Metal-binding; Myristate;
KW Repeat; Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..202
FT /note="S-modulin"
FT /id="PRO_0000073799"
FT DOMAIN 25..60
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 61..96
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 97..132
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 147..182
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT CONFLICT 91
FT /note="M -> H (in Ref. 1; BAA19728)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 23527 MW; 5FFE379649904A2B CRC64;
MGNTKSGALS KEILEELQLN TKFTQEELCT WYQSFLKECP SGRISKKQFE SIYSKFFPDA
DPKAYAQHVF RSFDANNDGT LDFKEYMIAL MMTSSGKANQ KLEWAFCLYD VDGNGTINKK
EVLEIITAIF KMINAEDQKH LPEDENTPEK RTNKIWVYFG KKDDDKLTEG EFIQGIVKNK
EILRLIQYEP QKVKDKLKEK KH
