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NFCP_HETCR
ID   NFCP_HETCR              Reviewed;         227 AA.
AC   Q95W85;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=GFP-like non-fluorescent chromoprotein;
DE   AltName: Full=HcRed;
DE   AltName: Full=hcCP;
OS   Heteractis crispa (Leathery sea anemone) (Radianthus macrodactylus).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Stichodactylidae; Heteractis.
OX   NCBI_TaxID=175771;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAL27538.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND MUTAGENESIS OF ALA-2; THR-36;
RP   LEU-122; CYS-143; LEU-173; PRO-201 AND LYS-204.
RX   PubMed=11682051; DOI=10.1016/s0014-5793(01)02930-1;
RA   Gurskaya N.G., Fradkov A.F., Terskikh A., Matz M.V., Labas Y.A.,
RA   Martynov V.I., Yanushevich Y.G., Lukyanov K.A., Lukyanov S.A.;
RT   "GFP-like chromoproteins as a source of far-red fluorescent proteins.";
RL   FEBS Lett. 507:16-20(2001).
CC   -!- FUNCTION: Non-fluorescent pigment protein that is lilac in color.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=578 nm;
CC         Note=Fluorescence excitation of HcRed mutant is at 592 nm and
CC         emission at 645 nm.;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11682051}.
CC   -!- PTM: Contains a chromophore consisting of modified amino acid residues.
CC       The chromophore is formed by autocatalytic backbone condensation
CC       between Xaa-N and Gly-(N+2), oxidation of Tyr-(N+1) to
CC       didehydrotyrosine, and formation of a double bond to the alpha-amino
CC       nitrogen of residue Xaa-N. Maturation of the chromophore requires
CC       nothing other than molecular oxygen. The precise stereochemistry of the
CC       tyrosine has not been determined.
CC   -!- BIOTECHNOLOGY: Fluorescent proteins have become a useful and ubiquitous
CC       tool for making chimeric proteins, where they function as a fluorescent
CC       protein tag. Typically they tolerate N- and C-terminal fusion to a
CC       broad variety of proteins. They have been expressed in most known cell
CC       types and are used as a noninvasive fluorescent marker in living cells
CC       and organisms. They enable a wide range of applications where they have
CC       functioned as a cell lineage tracer, reporter of gene expression, or as
CC       a measure of protein-protein interactions. {ECO:0000305}.
CC   -!- MISCELLANEOUS: In the wild-type form, the chromophore matures at 20
CC       degrees Celsius. Mutants have been selected to mature at 37 degrees
CC       Celsius to make them suitable for use in vivo and cell culture.
CC   -!- SIMILARITY: Belongs to the GFP family. {ECO:0000305}.
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DR   EMBL; AF363776; AAL27538.1; -; mRNA.
DR   PDB; 1YZW; X-ray; 2.10 A; A/B/C/D=1-227.
DR   PDB; 6DEJ; X-ray; 1.63 A; A/B/C/D=1-227.
DR   PDB; 6Y1G; X-ray; 2.30 A; A/B/C/D=2-227.
DR   PDBsum; 1YZW; -.
DR   PDBsum; 6DEJ; -.
DR   PDBsum; 6Y1G; -.
DR   AlphaFoldDB; Q95W85; -.
DR   SMR; Q95W85; -.
DR   EvolutionaryTrace; Q95W85; -.
DR   GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.155.10; -; 1.
DR   InterPro; IPR009017; GFP.
DR   InterPro; IPR011584; GFP-related.
DR   Pfam; PF01353; GFP; 1.
DR   SUPFAM; SSF54511; SSF54511; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chromophore; Luminescence; Photoprotein.
FT   CHAIN           1..227
FT                   /note="GFP-like non-fluorescent chromoprotein"
FT                   /id="PRO_0000192587"
FT   MOD_RES         64
FT                   /note="2,3-didehydrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P83690"
FT   CROSSLNK        63..65
FT                   /note="2-iminomethyl-5-imidazolinone (Glu-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:P83690"
FT   MUTAGEN         2
FT                   /note="A->S: In Hcred; matures at 37 degrees Celsius and
FT                   produces over 6-fold brighter fluorescence and a
FT                   homodimeric form; when associated with A-36; S-143; H-173;
FT                   L-201 and E-204."
FT                   /evidence="ECO:0000269|PubMed:11682051"
FT   MUTAGEN         36
FT                   /note="T->A: In Hcred; matures at 37 degrees Celsius and
FT                   produces over 6-fold brighter fluorescence and a
FT                   homodimeric form; when associated with S-2; S-143; H-173;
FT                   L-201 and E-204."
FT                   /evidence="ECO:0000269|PubMed:11682051"
FT   MUTAGEN         122
FT                   /note="L->H: Produces a dimeric form."
FT                   /evidence="ECO:0000269|PubMed:11682051"
FT   MUTAGEN         143
FT                   /note="C->S: In Hcred; matures at 37 degrees Celsius and
FT                   produces over 6-fold brighter fluorescence and a
FT                   homodimeric form; when associated with S-2; A-36; H-173; L-
FT                   201 and E-204."
FT                   /evidence="ECO:0000269|PubMed:11682051"
FT   MUTAGEN         173
FT                   /note="L->H: In Hcred; matures at 37 degrees Celsius and
FT                   produces over 6-fold brighter fluorescence and a
FT                   homodimeric form; when associated with S-2; A-36; S-143; L-
FT                   201 and E-204."
FT                   /evidence="ECO:0000269|PubMed:11682051"
FT   MUTAGEN         201
FT                   /note="P->L: In Hcred; matures at 37 degrees Celsius and
FT                   produces over 6-fold brighter fluorescence and a
FT                   homodimeric form; when associated with S-2; A-36; S-143; H-
FT                   173 and E-204."
FT                   /evidence="ECO:0000269|PubMed:11682051"
FT   MUTAGEN         204
FT                   /note="K->E: In Hcred; matures at 37 degrees Celsius and
FT                   produces over 6-fold brighter fluorescence and a
FT                   homodimeric form; when associated with S-2; A-36; S-143; H-
FT                   173 and L-201."
FT                   /evidence="ECO:0000269|PubMed:11682051"
FT   STRAND          7..19
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   STRAND          22..33
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   TURN            34..37
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   STRAND          38..48
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   HELIX           55..57
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   HELIX           79..82
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   TURN            83..86
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   STRAND          88..96
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   STRAND          101..111
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   STRAND          114..124
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   TURN            131..135
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   STRAND          143..150
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   STRAND          153..164
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   STRAND          167..181
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   HELIX           183..185
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   STRAND          191..204
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   TURN            205..207
FT                   /evidence="ECO:0007829|PDB:6DEJ"
FT   STRAND          208..218
FT                   /evidence="ECO:0007829|PDB:6DEJ"
SQ   SEQUENCE   227 AA;  25637 MW;  CB40899E95E7EC64 CRC64;
     MAGLLKESMR IKMYMEGTVN GHYFKCEGEG DGNPFTGTQS MRIHVTEGAP LPFAFDILAP
     CCEYGSRTFV HHTAEIPDFF KQSFPEGFTW ERTTTYEDGG ILTAHQDTSL EGNCLIYKVK
     VLGTNFPADG PVMKNKSGGW EPCTEVVYPE NGVLCGRNVM ALKVGDRRLI CHLYTSYRSK
     KAVRALTMPG FHFTDIRLQM PRKKKDEYFE LYEASVARYS DLPEKAN
 
 
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