OCP_SYNY3
ID OCP_SYNY3 Reviewed; 317 AA.
AC P74102;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Orange carotenoid-binding protein {ECO:0000303|PubMed:9398074};
DE Short=OCP {ECO:0000303|PubMed:9398074};
DE Contains:
DE RecName: Full=Red carotenoid-binding protein {ECO:0000303|PubMed:9398074};
DE Short=RCP {ECO:0000303|PubMed:9398074};
GN OrderedLocusNames=slr1963;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-60, MASS
RP SPECTROMETRY, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=9398074; DOI=10.1016/s0005-2728(97)00067-4;
RA Wu Y.P., Krogmann D.W.;
RT "The orange carotenoid protein of Synechocystis PCC 6803.";
RL Biochim. Biophys. Acta 1322:1-7(1997).
RN [2] {ECO:0000312|EMBL:BAA18188.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3] {ECO:0000305}
RP REVIEW.
RX PubMed=15325905; DOI=10.1016/j.abb.2004.03.018;
RA Kerfeld C.A.;
RT "Water-soluble carotenoid proteins of cyanobacteria.";
RL Arch. Biochem. Biophys. 430:2-9(2004).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=16531492; DOI=10.1105/tpc.105.040121;
RA Wilson A., Ajlani G., Verbavatz J.M., Vass I., Kerfeld C.A., Kirilovsky D.;
RT "A soluble carotenoid protein involved in phycobilisome-related energy
RT dissipation in cyanobacteria.";
RL Plant Cell 18:992-1007(2006).
RN [5]
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP TRP-110.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=18687902; DOI=10.1073/pnas.0804636105;
RA Wilson A., Punginelli C., Gall A., Bonetti C., Alexandre M.,
RA Routaboul J.M., Kerfeld C.A., van Grondelle R., Robert B., Kennis J.T.,
RA Kirilovsky D.;
RT "A photoactive carotenoid protein acting as light intensity sensor.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12075-12080(2008).
RN [6]
RP INTERACTION WITH FRP, SUBUNIT, AND INDUCTION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=20534537; DOI=10.1073/pnas.1002912107;
RA Boulay C., Wilson A., D'Haene S., Kirilovsky D.;
RT "Identification of a protein required for recovery of full antenna capacity
RT in OCP-related photoprotective mechanism in cyanobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11620-11625(2010).
RN [7]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TYR-44.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=21764991; DOI=10.1105/tpc.111.086884;
RA Gwizdala M., Wilson A., Kirilovsky D.;
RT "In vitro reconstitution of the cyanobacterial photoprotective mechanism
RT mediated by the orange carotenoid protein in Synechocystis PCC 6803.";
RL Plant Cell 23:2631-2643(2011).
RN [8]
RP FUNCTION, INTERACTION WITH FRP, SUBUNIT, AND DOMAIN.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=23716688; DOI=10.1073/pnas.1303673110;
RA Sutter M., Wilson A., Leverenz R.L., Lopez-Igual R., Thurotte A.,
RA Salmeen A.E., Kirilovsky D., Kerfeld C.A.;
RT "Crystal structure of the FRP and identification of the active site for
RT modulation of OCP-mediated photoprotection in cyanobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:10022-10027(2013).
RN [9]
RP POSSIBLE REACTION MECHANISM.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=21907180; DOI=10.1016/j.bbabio.2011.08.009;
RA Gorbunov M.Y., Kuzminov F.I., Fadeev V.V., Kim J.D., Falkowski P.G.;
RT "A kinetic model of non-photochemical quenching in cyanobacteria.";
RL Biochim. Biophys. Acta 1807:1591-1599(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-316 IN COMPLEX WITH CAROTENOID,
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS
RP OF TYR-44; TRP-110 AND ARG-155.
RX PubMed=20368334; DOI=10.1074/jbc.m110.115709;
RA Wilson A., Kinney J.N., Zwart P.H., Punginelli C., D'Haene S., Perreau F.,
RA Klein M.G., Kirilovsky D., Kerfeld C.A.;
RT "Structural determinants underlying photoprotection in the photoactive
RT orange carotenoid protein of cyanobacteria.";
RL J. Biol. Chem. 285:18364-18375(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 21-165 (RCP) IN COMPLEX WITH
RP CAROTENOID, X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-317 (OCP) IN
RP COMPLEX WITH CAROTENOID, COFACTOR, DOMAIN, AND MUTAGENESIS OF GLU-34;
RP CYS-84; PRO-126; 126-PRO--TYR-129 AND TYR-129.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=26113721; DOI=10.1126/science.aaa7234;
RA Leverenz R.L., Sutter M., Wilson A., Gupta S., Thurotte A.,
RA Bourcier de Carbon C., Petzold C.J., Ralston C., Perreau F., Kirilovsky D.,
RA Kerfeld C.A.;
RT "A 12 Angstrom carotenoid translocation in a photoswitch associated with
RT cyanobacterial photoprotection.";
RL Science 348:1463-1466(2015).
CC -!- FUNCTION: Acts as a blue-light photoreceptor and photo-protectant.
CC Essential for inhibiting damaged induced by excess blue-green light via
CC a process known as non-photochemical quenching (NPQ) (PubMed:16531492,
CC PubMed:18687902, PubMed:20368334). In the dark or dim light the stable
CC inactive form (OCP-O) is orange, upon illumination with blue-green
CC light it converts to a metastable active red form (OCP-R), inducing
CC energy dissipation, quenching cellular fluorescence via NPQ
CC (PubMed:18687902, PubMed:20368334). One OCP-R molecule is sufficient to
CC quench 1 phycobilisome (PubMed:21764991). More OCP-R accumulates under
CC high-light and low temperature; in the dark OCP-R spontaneously reverts
CC to OCP-O (PubMed:18687902). Reversion of OCP-O is accelerated by FRP
CC (PubMed:20534537, PubMed:23716688). A kinetic study suggests conversion
CC of OCP-O to OCP-R is limited by cis-trans proline isomerization of
CC either Gln224-Pro225 or Pro225-Pro226 (PubMed:21907180).
CC {ECO:0000269|PubMed:16531492, ECO:0000269|PubMed:18687902,
CC ECO:0000269|PubMed:20368334, ECO:0000269|PubMed:20534537,
CC ECO:0000269|PubMed:21764991, ECO:0000269|PubMed:21907180,
CC ECO:0000269|PubMed:23716688}.
CC -!- COFACTOR:
CC Name=3'-hydroxyechinenone; Xref=ChEBI:CHEBI:80214;
CC Evidence={ECO:0000269|PubMed:18687902, ECO:0000269|PubMed:20368334};
CC Note=Binds 1 carotenoid molecule per subunit (3'-hydroxyechinenone is
CC the physiological carotenoid, echinenone (70%), 3'-hydroxyechinenone
CC (16%) or zeaxanthin (14%) were all detected in overexpressed,
CC crystallized protein), makes contacts with both domains of the whole
CC protein (PubMed:20368334). Upon RCP generation the carotenoid
CC translocates 12 Angstroms into the N-terminal domain, altering its
CC binding and photochemical properties (PubMed:26113721).
CC {ECO:0000269|PubMed:20368334, ECO:0000269|PubMed:26113721};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=~495 nm;
CC Note=A double maxima at 467 and 495 nm is seen for the orange
CC (inactive) form, the red (active) form has a single maximum at ~505
CC nm. {ECO:0000269|PubMed:18687902, ECO:0000269|PubMed:20368334};
CC -!- SUBUNIT: Monomer (PubMed:20368334). Interacts with the APC core of the
CC phycobilisome (PB), probably at a ratio of 1:1 in a light-independent
CC manner; possibly only OCP-R binds to PBs. Interacts with FRP
CC (PubMed:20534537, PubMed:23716688). Detachment from PBs is accelerated
CC by FPR (PubMed:21764991). {ECO:0000269|PubMed:20368334,
CC ECO:0000269|PubMed:20534537, ECO:0000269|PubMed:21764991,
CC ECO:0000269|PubMed:23716688}.
CC -!- INTERACTION:
CC P74102; P74103: frp; NbExp=2; IntAct=EBI-1618104, EBI-1618115;
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:16531492}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:16531492}.
CC Note=Associated with the phycobilisome on the cytoplasmic side of the
CC thylakoid membrane (PubMed:16531492). {ECO:0000269|PubMed:16531492}.
CC -!- INDUCTION: Transcribed from its own promoter, it may also be
CC cotranscribed with downstream frp. {ECO:0000269|PubMed:20534537}.
CC -!- DOMAIN: Binds FRP via the C-terminal domain (residues 170-317)
CC (PubMed:23716688). Upon RCP generation the carotenoid translocates 12
CC Angstroms into the N-terminal domain, altering its binding and
CC photochemical properties (PubMed:26113721).
CC {ECO:0000269|PubMed:23716688, ECO:0000269|PubMed:26113721}.
CC -!- PTM: Proteolytically cleaved into a red 16.7 kDa form named red
CC carotenoid-binding protein (RCP) which lacks 15 residues from the N-
CC terminus and approximately 150 residues from the C-terminus
CC (PubMed:9398074). {ECO:0000269|PubMed:9398074}.
CC -!- MASS SPECTROMETRY: [Orange carotenoid-binding protein]: Mass=34622;
CC Method=MALDI; Note=OCP.; Evidence={ECO:0000269|PubMed:9398074};
CC -!- MASS SPECTROMETRY: [Red carotenoid-binding protein]: Mass=16739;
CC Method=MALDI; Note=RCP.; Evidence={ECO:0000269|PubMed:9398074};
CC -!- DISRUPTION PHENOTYPE: Loss of NPQ induced by strong white or blue-green
CC light, cells are more sensitive to high light.
CC {ECO:0000269|PubMed:16531492}.
CC -!- SIMILARITY: Belongs to the orange carotenoid-binding protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU01109, ECO:0000305}.
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DR EMBL; BA000022; BAA18188.1; -; Genomic_DNA.
DR PIR; S75627; S75627.
DR PDB; 3MG1; X-ray; 1.65 A; A/B=1-316.
DR PDB; 3MG2; X-ray; 2.65 A; A/B=1-316.
DR PDB; 3MG3; X-ray; 1.70 A; A/B=1-316.
DR PDB; 4XB4; X-ray; 1.54 A; A/B=21-165.
DR PDB; 4XB5; X-ray; 1.90 A; A=2-317.
DR PDB; 5TUW; X-ray; 2.30 A; A/B/C/D/E/F=1-317.
DR PDB; 5TUX; X-ray; 1.50 A; A=1-317.
DR PDB; 5TV0; X-ray; 1.65 A; A=1-317.
DR PDB; 6T6K; X-ray; 1.37 A; A=1-317.
DR PDB; 6T6M; X-ray; 1.49 A; A=1-317.
DR PDB; 6T6O; X-ray; 1.40 A; A=1-317.
DR PDBsum; 3MG1; -.
DR PDBsum; 3MG2; -.
DR PDBsum; 3MG3; -.
DR PDBsum; 4XB4; -.
DR PDBsum; 4XB5; -.
DR PDBsum; 5TUW; -.
DR PDBsum; 5TUX; -.
DR PDBsum; 5TV0; -.
DR PDBsum; 6T6K; -.
DR PDBsum; 6T6M; -.
DR PDBsum; 6T6O; -.
DR AlphaFoldDB; P74102; -.
DR SASBDB; P74102; -.
DR SMR; P74102; -.
DR DIP; DIP-59343N; -.
DR IntAct; P74102; 2.
DR STRING; 1148.1653273; -.
DR PaxDb; P74102; -.
DR EnsemblBacteria; BAA18188; BAA18188; BAA18188.
DR KEGG; syn:slr1963; -.
DR eggNOG; COG3631; Bacteria.
DR InParanoid; P74102; -.
DR OMA; PFQRPIV; -.
DR PhylomeDB; P74102; -.
DR EvolutionaryTrace; P74102; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031404; F:chloride ion binding; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0016037; P:light absorption; IEA:InterPro.
DR Gene3D; 1.10.2090.10; -; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR015233; Orange_carotenoid-bd_N.
DR InterPro; IPR036917; Orange_carotenoid-bd_N_sf.
DR Pfam; PF09150; Carot_N; 1.
DR Pfam; PF02136; NTF2; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF81930; SSF81930; 1.
DR PROSITE; PS51773; OCP_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antenna complex; Chromophore; Direct protein sequencing;
KW Membrane; Photoreceptor protein; Phycobilisome; Receptor;
KW Reference proteome; Sensory transduction; Thylakoid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9398074"
FT CHAIN 2..317
FT /note="Orange carotenoid-binding protein"
FT /evidence="ECO:0000269|PubMed:9398074"
FT /id="PRO_0000282352"
FT CHAIN 16..?
FT /note="Red carotenoid-binding protein"
FT /evidence="ECO:0000269|PubMed:9398074"
FT /id="PRO_0000282353"
FT DOMAIN 18..169
FT /note="OCP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01109"
FT BINDING 34..38
FT /ligand="echinenone"
FT /ligand_id="ChEBI:CHEBI:4746"
FT /note="only in form RCP"
FT /evidence="ECO:0000269|PubMed:26113721"
FT BINDING 37..44
FT /ligand="echinenone"
FT /ligand_id="ChEBI:CHEBI:4746"
FT /note="in forms OCP and RCP"
FT /evidence="ECO:0000269|PubMed:20368334,
FT ECO:0000269|PubMed:26113721"
FT BINDING 80..83
FT /ligand="echinenone"
FT /ligand_id="ChEBI:CHEBI:4746"
FT /note="only in form RCP"
FT /evidence="ECO:0000269|PubMed:26113721"
FT BINDING 107..117
FT /ligand="echinenone"
FT /ligand_id="ChEBI:CHEBI:4746"
FT /note="in forms OCP and RCP"
FT /evidence="ECO:0000269|PubMed:20368334,
FT ECO:0000269|PubMed:26113721"
FT BINDING 125..129
FT /ligand="echinenone"
FT /ligand_id="ChEBI:CHEBI:4746"
FT /note="only in form RCP"
FT /evidence="ECO:0000269|PubMed:26113721"
FT BINDING 151..161
FT /ligand="echinenone"
FT /ligand_id="ChEBI:CHEBI:4746"
FT /note="residues alter contact in forms OCP and RCP"
FT /evidence="ECO:0000269|PubMed:20368334,
FT ECO:0000269|PubMed:26113721"
FT BINDING 201
FT /ligand="echinenone"
FT /ligand_id="ChEBI:CHEBI:4746"
FT /note="only in form OCP"
FT /evidence="ECO:0000269|PubMed:20368334,
FT ECO:0000269|PubMed:26113721"
FT BINDING 245..250
FT /ligand="echinenone"
FT /ligand_id="ChEBI:CHEBI:4746"
FT /note="only in form OCP"
FT /evidence="ECO:0000269|PubMed:20368334,
FT ECO:0000269|PubMed:26113721"
FT BINDING 273..284
FT /ligand="echinenone"
FT /ligand_id="ChEBI:CHEBI:4746"
FT /note="only in form OCP"
FT /evidence="ECO:0000269|PubMed:20368334,
FT ECO:0000269|PubMed:26113721"
FT BINDING 288
FT /ligand="echinenone"
FT /ligand_id="ChEBI:CHEBI:4746"
FT /note="only in form OCP"
FT /evidence="ECO:0000269|PubMed:20368334,
FT ECO:0000269|PubMed:26113721"
FT MUTAGEN 34
FT /note="E->A: Alters carotenoid specificity, <40% quenching,
FT decreases stability of OCP-R, accelerates OCP-R to OCP-O
FT reversion."
FT /evidence="ECO:0000269|PubMed:26113721"
FT MUTAGEN 44
FT /note="Y->F: Acts like wild-type."
FT /evidence="ECO:0000269|PubMed:20368334"
FT MUTAGEN 44
FT /note="Y->S: Cannot convert to red form (OCP-R), no NPQ.
FT Does not bind to phycobilisomes."
FT /evidence="ECO:0000269|PubMed:20368334,
FT ECO:0000269|PubMed:21764991"
FT MUTAGEN 84
FT /note="C->A: <40% quenching, decreases stability of OCP-R,
FT accelerates OCP-R to OCP-O reversion."
FT /evidence="ECO:0000269|PubMed:26113721"
FT MUTAGEN 110
FT /note="W->F: Acts like wild-type."
FT /evidence="ECO:0000269|PubMed:20368334"
FT MUTAGEN 110
FT /note="W->S: Incomplete conversion to red form (OCP-R), no
FT NPQ."
FT /evidence="ECO:0000269|PubMed:18687902,
FT ECO:0000269|PubMed:20368334"
FT MUTAGEN 126..129
FT /note="PAGY->VAGF: Cannot convert to red form (OCP-R)."
FT /evidence="ECO:0000269|PubMed:26113721"
FT MUTAGEN 126
FT /note="P->V: <40% quenching, decreases stability of OCP-R,
FT accelerates OCP-R to OCP-O reversion."
FT /evidence="ECO:0000269|PubMed:26113721"
FT MUTAGEN 129
FT /note="Y->F: <40% quenching, decreases stability of OCP-R,
FT accelerates OCP-R to OCP-O reversion."
FT /evidence="ECO:0000269|PubMed:26113721"
FT MUTAGEN 155
FT /note="R->L: Able to convert to red form (OCP-R), no NPQ."
FT /evidence="ECO:0000269|PubMed:20368334"
FT CONFLICT 73
FT /note="A -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="G -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="F -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="A -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="G -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:6T6K"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:6T6K"
FT HELIX 33..47
FT /evidence="ECO:0007829|PDB:6T6K"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:6T6K"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:4XB4"
FT HELIX 58..72
FT /evidence="ECO:0007829|PDB:6T6K"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:6T6K"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:6T6K"
FT HELIX 103..118
FT /evidence="ECO:0007829|PDB:6T6K"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:6T6K"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:6T6K"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:4XB5"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:6T6K"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:6T6K"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:6T6K"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:6T6K"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:6T6K"
FT HELIX 234..244
FT /evidence="ECO:0007829|PDB:6T6K"
FT STRAND 249..258
FT /evidence="ECO:0007829|PDB:6T6K"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:6T6O"
FT STRAND 265..274
FT /evidence="ECO:0007829|PDB:6T6K"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:6T6K"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:6T6K"
FT STRAND 284..292
FT /evidence="ECO:0007829|PDB:6T6K"
FT STRAND 298..308
FT /evidence="ECO:0007829|PDB:6T6K"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:6T6K"
SQ SEQUENCE 317 AA; 34659 MW; 8FF633BDE6D530F2 CRC64;
MPFTIDSARG IFPNTLAADV VPATIARFSQ LNAEDQLALI WFAYLEMGKT LTIAAPGAAS
MQLAENALKE IQAMGPLQQT QAMCDLANRA DTPLCRTYAS WSPNIKLGFW YRLGELMEQG
FVAPIPAGYQ LSANANAVLA TIQGLESGQQ ITVLRNAVVD MGFTAGKDGK RIAEPVVPPQ
DTASRTKVSI EGVTNATVLN YMDNLNANDF DTLIELFTSD GALQPPFQRP IVGKENVLRF
FREECQNLKL IPERGVTEPA EDGFTQIKVT GKVQTPWFGG NVGMNIAWRF LLNPEGKIFF
VAIDLLASPK ELLNFAR
