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GFP-like non-fluorescent chromoprotein (HcRed) (hcCP)

 NFCP_HETCR              Reviewed;         227 AA.
Q95W85;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
10-MAY-2017, entry version 57.
RecName: Full=GFP-like non-fluorescent chromoprotein;
AltName: Full=HcRed;
AltName: Full=hcCP;
Heteractis crispa (Leathery sea anemone) (Radianthus macrodactylus).
Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
Stichodactylidae; Heteractis.
NCBI_TaxID=175771;
[1] {ECO:0000305, ECO:0000312|EMBL:AAL27538.1}
NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND MUTAGENESIS OF ALA-2; THR-36;
LEU-122; CYS-143; LEU-173; PRO-201 AND LYS-204.
PubMed=11682051; DOI=10.1016/S0014-5793(01)02930-1;
Gurskaya N.G., Fradkov A.F., Terskikh A., Matz M.V., Labas Y.A.,
Martynov V.I., Yanushevich Y.G., Lukyanov K.A., Lukyanov S.A.;
"GFP-like chromoproteins as a source of far-red fluorescent
proteins.";
FEBS Lett. 507:16-20(2001).
-!- FUNCTION: Non-fluorescent pigment protein that is lilac in color.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=578 nm;
Note=Fluorescence excitation of HcRed mutant is at 592 nm and
emission at 645 nm.;
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11682051}.
-!- PTM: Contains a chromophore consisting of modified amino acid
residues. The chromophore is formed by autocatalytic backbone
condensation between Xaa-N and Gly-(N+2), oxidation of Tyr-(N+1)
to didehydrotyrosine, and formation of a double bond to the alpha-
amino nitrogen of residue Xaa-N. Maturation of the chromophore
requires nothing other than molecular oxygen. The precise
stereochemistry of the tyrosine has not been determined.
-!- BIOTECHNOLOGY: Fluorescent proteins have become a useful and
ubiquitous tool for making chimeric proteins, where they function
as a fluorescent protein tag. Typically they tolerate N- and C-
terminal fusion to a broad variety of proteins. They have been
expressed in most known cell types and are used as a noninvasive
fluorescent marker in living cells and organisms. They enable a
wide range of applications where they have functioned as a cell
lineage tracer, reporter of gene expression, or as a measure of
protein-protein interactions. {ECO:0000305}.
-!- MISCELLANEOUS: In the wild-type form, the chromophore matures at
20 degrees Celsius. Mutants have been selected to mature at 37
degrees Celsius to make them suitable for use in vivo and cell
culture.
-!- SIMILARITY: Belongs to the GFP family. {ECO:0000305}.
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EMBL; AF363776; AAL27538.1; -; mRNA.
PDB; 1YZW; X-ray; 2.10 A; A/B/C/D=1-227.
PDBsum; 1YZW; -.
ProteinModelPortal; Q95W85; -.
SMR; Q95W85; -.
EvolutionaryTrace; Q95W85; -.
GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
InterPro; IPR009017; GFP.
InterPro; IPR011584; GFP-related.
Pfam; PF01353; GFP; 1.
SUPFAM; SSF54511; SSF54511; 1.
1: Evidence at protein level;
3D-structure; Chromophore; Luminescence; Photoprotein.
CHAIN 1 227 GFP-like non-fluorescent chromoprotein.
/FTId=PRO_0000192587.
MOD_RES 64 64 2,3-didehydrotyrosine.
{ECO:0000250|UniProtKB:P83690}.
CROSSLNK 63 65 2-iminomethyl-5-imidazolinone (Glu-Gly).
{ECO:0000250|UniProtKB:P83690}.
MUTAGEN 2 2 A->S: In Hcred; matures at 37 degrees
Celsius and produces over 6-fold brighter
fluorescence and a homodimeric form; when
associated with A-36; S-143; H-173; L-201
and E-204. {ECO:0000269|PubMed:11682051}.
MUTAGEN 36 36 T->A: In Hcred; matures at 37 degrees
Celsius and produces over 6-fold brighter
fluorescence and a homodimeric form; when
associated with S-2; S-143; H-173; L-201
and E-204. {ECO:0000269|PubMed:11682051}.
MUTAGEN 122 122 L->H: Produces a dimeric form.
{ECO:0000269|PubMed:11682051}.
MUTAGEN 143 143 C->S: In Hcred; matures at 37 degrees
Celsius and produces over 6-fold brighter
fluorescence and a homodimeric form; when
associated with S-2; A-36; H-173; L-201
and E-204. {ECO:0000269|PubMed:11682051}.
MUTAGEN 173 173 L->H: In Hcred; matures at 37 degrees
Celsius and produces over 6-fold brighter
fluorescence and a homodimeric form; when
associated with S-2; A-36; S-143; L-201
and E-204. {ECO:0000269|PubMed:11682051}.
MUTAGEN 201 201 P->L: In Hcred; matures at 37 degrees
Celsius and produces over 6-fold brighter
fluorescence and a homodimeric form; when
associated with S-2; A-36; S-143; H-173
and E-204. {ECO:0000269|PubMed:11682051}.
MUTAGEN 204 204 K->E: In Hcred; matures at 37 degrees
Celsius and produces over 6-fold brighter
fluorescence and a homodimeric form; when
associated with S-2; A-36; S-143; H-173
and L-201. {ECO:0000269|PubMed:11682051}.
STRAND 7 19 {ECO:0000244|PDB:1YZW}.
STRAND 22 33 {ECO:0000244|PDB:1YZW}.
TURN 34 37 {ECO:0000244|PDB:1YZW}.
STRAND 38 48 {ECO:0000244|PDB:1YZW}.
HELIX 55 61 {ECO:0000244|PDB:1YZW}.
HELIX 79 82 {ECO:0000244|PDB:1YZW}.
TURN 83 86 {ECO:0000244|PDB:1YZW}.
STRAND 88 96 {ECO:0000244|PDB:1YZW}.
STRAND 101 111 {ECO:0000244|PDB:1YZW}.
STRAND 114 124 {ECO:0000244|PDB:1YZW}.
TURN 131 135 {ECO:0000244|PDB:1YZW}.
STRAND 143 150 {ECO:0000244|PDB:1YZW}.
STRAND 153 164 {ECO:0000244|PDB:1YZW}.
STRAND 167 181 {ECO:0000244|PDB:1YZW}.
HELIX 183 185 {ECO:0000244|PDB:1YZW}.
STRAND 191 200 {ECO:0000244|PDB:1YZW}.
STRAND 202 204 {ECO:0000244|PDB:1YZW}.
TURN 205 207 {ECO:0000244|PDB:1YZW}.
STRAND 208 218 {ECO:0000244|PDB:1YZW}.
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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