ID   SYMPP_STHOU             Reviewed;         501 AA.
AC   C6KYS2; C6KYS3;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Symplectin {ECO:0000303|PubMed:12054553, ECO:0000303|PubMed:18997450};
DE            EC=3.5.-.-;
GN   Name=sympp {ECO:0000312|EMBL:BAH89067.1};
OS   Sthenoteuthis oualaniensis (Purpleback flying squid) (Symplectoteuthis
OS   oualaniensis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Decapodiformes; Teuthida; Oegopsina; Ommastrephidae;
OC   Sthenoteuthis.
OX   NCBI_TaxID=34553;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-20; 36-49; 55-66; 90-106; 114-126; 132-170; 178-190
RP   AND 212-230, AND FUNCTION.
RC   TISSUE=Photogenic organ {ECO:0000269|PubMed:12054553};
RX   PubMed=12054553; DOI=10.1016/s0006-291x(02)00296-6;
RA   Fujii T., Ahn J.Y., Kuse M., Mori H., Matsuda T., Isobe M.;
RT   "A novel photoprotein from oceanic squid (Symplectoteuthis oualaniensis)
RT   with sequence similarity to mammalian carbon-nitrogen hydrolase domains.";
RL   Biochem. Biophys. Res. Commun. 293:874-879(2002).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAH89067.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-501.
RC   TISSUE=Photogenic organ {ECO:0000312|EMBL:BAH89067.1};
RA   Ohsima K., Isobe M., Matsuda T.;
RT   "A photoprotein of luminous squid.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   FUNCTION, TISSUE SPECIFICITY, AND POST-TRANSLATIONAL MODIFICATION.
RX   PubMed=18997450; DOI=10.2183/pjab/84.386;
RA   Isobe M., Kuse M., Tani N., Fujii T., Matsuda T.;
RT   "Cysteine-390 is the binding site of luminous substance with symplectin, a
RT   photoprotein from Okinawan squid, Symplectoteuthis oualaniensis.";
RL   Proc. Jpn. Acad., B, Phys. Biol. Sci. 84:386-392(2008).
CC   -!- FUNCTION: Monovalent ion-dependent bioluminescence photoprotein.
CC       Displays an emission peak at 470 nm (blue light). Trace amounts of
CC       monovalent ion trigger the intramolecular oxidation of the chromophore,
CC       didehydrocoelenterazine, with the emission of light.
CC       {ECO:0000269|PubMed:12054553, ECO:0000269|PubMed:18997450}.
CC   -!- TISSUE SPECIFICITY: Photogenic gland (at protein level).
CC       {ECO:0000269|PubMed:12054553, ECO:0000269|PubMed:18997450}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined MW of this protein is: 60
CC       kDa. {ECO:0000269|PubMed:12054553}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       BTD/VNN family. {ECO:0000305}.
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DR   EMBL; AB447990; BAH89067.1; -; mRNA.
DR   EMBL; AB447991; BAH89068.1; -; mRNA.
DR   AlphaFoldDB; C6KYS2; -.
DR   SMR; C6KYS2; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008218; P:bioluminescence; IDA:UniProtKB.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.60.110.10; -; 1.
DR   InterPro; IPR040154; Biotinidase/VNN.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR043957; Vanin_C.
DR   PANTHER; PTHR10609; PTHR10609; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   Pfam; PF19018; Vanin_C; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Luminescence; Photoprotein;
KW   Potassium; Sodium.
FT   CHAIN           1..501
FT                   /note="Symplectin"
FT                   /id="PRO_0000395599"
FT   DOMAIN          20..287
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        163
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        196
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O25836,
FT                   ECO:0000255|PROSITE-ProRule:PRU00054"
FT   MOD_RES         390
FT                   /note="S-(coelenterazin-3a-yl)cysteine"
FT                   /evidence="ECO:0000269|PubMed:18997450"
FT   CONFLICT        80
FT                   /note="K -> R (in Ref. 2; BAH89068)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86
FT                   /note="H -> L (in Ref. 2; BAH89068)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="W -> N (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        186
FT                   /note="T -> I (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="E -> D (in Ref. 2; BAH89068)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        439
FT                   /note="E -> V (in Ref. 2; BAH89068)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        474..475
FT                   /note="SH -> PN (in Ref. 2; BAH89068)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   501 AA;  57486 MW;  7E232E263D182AF4 CRC64;
     YVRPVSSWKV AVFEHQVIPP KTDMETREEA LDALKLNSDV YHEAVLESRS KGVKMIVFPE
     YGLYDINTLT RTRMDLMAEK VPHPKHGHRN PCDEPEYQTQ SSEMLRTFSC MAKENDMYMV
     VNMAGREPCR RATEPECPGD KQLLYNTNVA FNNEGDVVAR YYKTHLFWEE GWFNSSKNYE
     MALWDTPIGK FGTFMCFDFQ AVQLIEQYNV RHIAYPASWV NLPPIYQSIQ SHSAFARFAK
     INLLAASVHR LETSTYGSGI YSPNGAEIFY FRPDIPKSKL LVAEILPIHV KKPEQTVVNF
     DNPVFPSEDD DVQDLFDRGD FAFLKYKRMT TRAGTVEVCQ KSFCCKARYA VKDRFKEVYA
     VGVYDGLLSA GANNLYFQIC TVIQCPHKKC GLKISKVRTH FKYLNLRADG WLDRYVFPSY
     TVMYNNYIAL DPFVWNYTEA GGIETKPGTS TPLHSANLVA RIYAKDSSKH VHQSHPIDEG
     VIKMAVKYML YVMAAYVYAA S