HCYG_ENTDO
ID HCYG_ENTDO Reviewed; 2896 AA.
AC O61363;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Hemocyanin G-type, units Oda to Odg;
GN Name=ODHCY;
OS Enteroctopus dofleini (North Pacific giant octopus) (Octopus dofleini).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Enteroctopus.
OX NCBI_TaxID=267067;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Branchial gland;
RX PubMed=9614945; DOI=10.1006/jmbi.1998.1648;
RA Miller K.I., Cuff M.E., Lang W.F., Varga-Weisz P., Field K.G.,
RA van Holde K.E.;
RT "Sequence of the Octopus dofleini hemocyanin subunit: structural and
RT evolutionary implications.";
RL J. Mol. Biol. 278:827-842(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF SUBUNIT ODG IN COMPLEX WITH
RP COPPER, AND DISULFIDE BOND.
RX PubMed=9614947; DOI=10.1006/jmbi.1998.1647;
RA Cuff M.E., Miller K.I., van Holde K.E., Hendrickson W.A.;
RT "Crystal structure of a functional unit from Octopus hemocyanin.";
RL J. Mol. Biol. 278:855-870(1998).
CC -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC freely dissolved in the hemolymph of many mollusks and arthropods.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Note=Binds 2 copper ions per heterodimer.;
CC -!- SUBUNIT: Decamers of large identical subunits (350 kDa), each
CC containing 7 globular oxygen-binding functional units: ODA, ODB, ODC,
CC ODD, ODE, ODF, and ODG. Decamer formation requires the presence of
CC magnesium ions.
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000305}.
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DR EMBL; AF020548; AAC39018.1; -; mRNA.
DR PIR; S13442; S13442.
DR PIR; T30939; T30939.
DR PDB; 1JS8; X-ray; 2.30 A; A/B=2503-2896.
DR PDBsum; 1JS8; -.
DR SMR; O61363; -.
DR PRIDE; O61363; -.
DR EvolutionaryTrace; O61363; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1280.10; -; 7.
DR Gene3D; 2.60.310.10; -; 7.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR028999; Haemocyanin_beta-sandwich.
DR InterPro; IPR036848; Haemocyanin_C_sf.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF14830; Haemocyan_bet_s; 7.
DR Pfam; PF00264; Tyrosinase; 8.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 7.
DR SUPFAM; SSF81277; SSF81277; 7.
DR PROSITE; PS00497; TYROSINASE_1; 7.
DR PROSITE; PS00498; TYROSINASE_2; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Disulfide bond; Glycoprotein; Metal-binding;
KW Oxygen transport; Repeat; Thioether bond; Transport.
FT CHAIN 1..2896
FT /note="Hemocyanin G-type, units Oda to Odg"
FT /id="PRO_0000204301"
FT REGION 1..419
FT /note="Functional unit Oda"
FT /evidence="ECO:0000305|PubMed:9614947"
FT REGION 420..834
FT /note="Functional unit Odb"
FT /evidence="ECO:0000305|PubMed:9614947"
FT REGION 835..1254
FT /note="Functional unit Odc"
FT /evidence="ECO:0000305|PubMed:9614947"
FT REGION 1255..1667
FT /note="Functional unit Odd"
FT /evidence="ECO:0000305|PubMed:9614947"
FT REGION 1668..2085
FT /note="Functional unit Ode"
FT /evidence="ECO:0000305|PubMed:9614947"
FT REGION 2086..2502
FT /note="Functional unit Odf"
FT /evidence="ECO:0000305|PubMed:9614947"
FT REGION 2503..2896
FT /note="Functional unit Odg"
FT /evidence="ECO:0000305|PubMed:9614947"
FT BINDING 41
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 601
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 605
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 632
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 875
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 895
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 904
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 1013
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 1017
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 1044
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 1292
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 1312
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 1321
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 1425
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 1429
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 1456
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 1708
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 1728
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 1737
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 1849
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 1853
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 1880
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 2126
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 2144
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 2153
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 2262
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 2266
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 2293
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 2543
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0007744|PDB:1JS8"
FT BINDING 2562
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0007744|PDB:1JS8"
FT BINDING 2571
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0007744|PDB:1JS8"
FT BINDING 2671
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0007744|PDB:1JS8"
FT BINDING 2675
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0007744|PDB:1JS8"
FT BINDING 2702
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0007744|PDB:1JS8"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 804
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1634
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2055
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2553
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 47..57
FT /evidence="ECO:0000250"
FT DISULFID 168..234
FT /evidence="ECO:0000250"
FT DISULFID 321..333
FT /evidence="ECO:0000250"
FT DISULFID 466..477
FT /evidence="ECO:0000250"
FT DISULFID 591..657
FT /evidence="ECO:0000250"
FT DISULFID 881..892
FT /evidence="ECO:0000250"
FT DISULFID 1003..1070
FT /evidence="ECO:0000250"
FT DISULFID 1298..1309
FT /evidence="ECO:0000250"
FT DISULFID 1415..1482
FT /evidence="ECO:0000250"
FT DISULFID 1571..1581
FT /evidence="ECO:0000250"
FT DISULFID 1714..1725
FT /evidence="ECO:0000250"
FT DISULFID 1839..1906
FT /evidence="ECO:0000250"
FT DISULFID 1997..2003
FT /evidence="ECO:0000250"
FT DISULFID 2131..2141
FT /evidence="ECO:0000250"
FT DISULFID 2252..2319
FT /evidence="ECO:0000250"
FT DISULFID 2406..2411
FT /evidence="ECO:0000250"
FT DISULFID 2549..2559
FT /evidence="ECO:0000269|PubMed:9614947,
FT ECO:0007744|PDB:1JS8"
FT DISULFID 2661..2728
FT /evidence="ECO:0000269|PubMed:9614947,
FT ECO:0007744|PDB:1JS8"
FT DISULFID 2815..2821
FT /evidence="ECO:0000269|PubMed:9614947,
FT ECO:0007744|PDB:1JS8"
FT CROSSLNK 58..60
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250"
FT CROSSLNK 478..480
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250"
FT CROSSLNK 893..895
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250"
FT CROSSLNK 1310..1312
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250"
FT CROSSLNK 1726..1728
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250"
FT CROSSLNK 2142..2144
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250"
FT CROSSLNK 2560..2562
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT STRAND 2504..2506
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2509..2511
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2514..2529
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2536..2540
FT /evidence="ECO:0007829|PDB:1JS8"
FT TURN 2541..2543
FT /evidence="ECO:0007829|PDB:1JS8"
FT STRAND 2544..2546
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2567..2584
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2605..2608
FT /evidence="ECO:0007829|PDB:1JS8"
FT TURN 2621..2624
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2633..2635
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2646..2656
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2660..2679
FT /evidence="ECO:0007829|PDB:1JS8"
FT TURN 2689..2691
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2692..2694
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2697..2719
FT /evidence="ECO:0007829|PDB:1JS8"
FT STRAND 2727..2729
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2732..2734
FT /evidence="ECO:0007829|PDB:1JS8"
FT TURN 2738..2741
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2748..2752
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2756..2758
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2762..2765
FT /evidence="ECO:0007829|PDB:1JS8"
FT STRAND 2767..2770
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2779..2789
FT /evidence="ECO:0007829|PDB:1JS8"
FT STRAND 2794..2799
FT /evidence="ECO:0007829|PDB:1JS8"
FT STRAND 2808..2816
FT /evidence="ECO:0007829|PDB:1JS8"
FT STRAND 2821..2829
FT /evidence="ECO:0007829|PDB:1JS8"
FT STRAND 2844..2847
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2849..2854
FT /evidence="ECO:0007829|PDB:1JS8"
FT STRAND 2863..2874
FT /evidence="ECO:0007829|PDB:1JS8"
FT HELIX 2879..2881
FT /evidence="ECO:0007829|PDB:1JS8"
FT STRAND 2886..2890
FT /evidence="ECO:0007829|PDB:1JS8"
SQ SEQUENCE 2896 AA; 331922 MW; BE1F35C8C987FBFC CRC64;
NLIRKDVDAL SEDEVLNLQV ALRAMQDDET PTGYQAIAAY HGEPADCKAP DGSTVVCCLH
GMPTFPLWHR LYTVQFEQTM VAHGSKLGVP YWDWTQPLNH LPELVSHPLF MDPTAHKAKK
NVFYSGDIAF EKKTTARAVD TRLFQASKGG KNFLLEGVLS ALEQDDYCHF EVQFEVAHNP
IHYLVGGRFT HSMSSLEYTS YDPLFFLHHS NVERLFTIWQ ALQKHRGLDG NANCGLNMFH
KPMEPFGRDT NPISLTKEHA KAVDVFNYNE LGYDYDDLHL NGMDIPELDT MLKERQQHPR
SFANFRLGGI KTSANVRVAV CIPSEDKRHS DNCNNHVGSF FILGGVHEMT WDFGYPFLFE
ITDVVKSLGI PLDGNYYVHA DVTEINGTLL PDGTIPRPTV SYIPHNFKDA DMVVVDKTGL
NVRKDLQSLT TEEEYELRVA MERFMDDKSI DGYQALAEFH GLPAKCPEPD AINRVACCVH
GMSTFPHWHR LVVMQFEDAL LARGSPIGVP YWDWTTPSSS LPHLVAVETY EDPYTKEVKP
NPFYHAQIEF LHNDVFTARN VDSRLFEKPT KGHHGYLHDG MLLAFEQEDF CDFEVQFEVT
HNAIHAWVGG NEPYSMSSLH YTSFDPLFWL HHSQVDRLWA VWQALQIYRG KPYKPYCALS
EVHRPLKPFA FEPPLNNNKH THSHSVPTHV YDYQSDLHYT YDTLFFGGMS VRELQRHIEE
DKAKDRVFVG FLLMGIKTSA NVVINVESAG NTYMAGTITI LGGSKEMEWR FDRLYKYEIT
DALAELGVDM HAEYSINLQI NDINGTALPP TSIPDPIVIF SPGKKESGVV FDELYRSRRD
VSSLTDADMN ALRKALQAYE DDKDASGYQQ VAAFHGSTKW CPSPDAEVKY ACCHHGMATF
PHWHRLLTVN FENGLRHNGY QNGIPYWDWT RPLSELPTLV KDETYADENG ETHPNPFFSG
VIDEIGEHTT RSPNPTLFLK PPFGHFTPLG DEVMYALEQE DFCSFEVQFE IAHNHIHALV
GGTEPYSMSS LEYTTFDPIF ILHHSNVDRI WAIWQALQKF RGHRYNSANC AIETLRKPMS
PFSLTSDINI DPMTREHSVP FDVFDYKKNF HYEYDLLELN GLSIPQLHRE ISRRRAKSRI
FATFMLEGIK QSALVEYYIR AHGSTDQLKA GEFYILGSAN EMPWKFDRVY KADITQQMKE
ANLHFNDQYH IEYHLKDLSG NEIAGVHLET AIIYEPGLGN FGEAGIWVEP VTSANRIRKN
LNALTDGDME SLRKAFKDMT TDGRYEEIAS FHGLPAQCPN KDGSKVYTCC IHGMPTFPHW
HRLYVALVEN ELLARGSGVA VPYWDWVQPF DHLPALVNRA TYYNSRTLLV EPNPFFKGKI
SFLNSETNRD PQEELFGNKY LYEHTLFVLE QTDFCDFEVH FEVLHNTIHS WLGGRDPHSM
SSLDFAAYDP IFFLHHSNID RIWAIWQELQ RYRKLPYNEA NCALPLLNVP MRPFSNTTAN
HDRMTLTHSA PNDVFDYQNV LHYKYDTLSF YDLTITQLDH LIEERKSHDR IFAGFLLHGV
QASADIHVFI CVPTSKHEEN CAHDVGVFSV LGGKSEMPWQ FASVFQYEIT DQLKLLGLNQ
NSHFRGVTEV TAVNGSSINS DIFPHPTIIY VPKQDHSADI KSEEGNEYLV RKNVERLSLS
EMNSLIHAFR RMQRDKSSDG FEAIASFHAL PPLCPSPTAK HRHACCLHGM ATFPHWHRLY
VVQFEQALHR HGATVGVPYW DWTRPISKIP DFIASKRYSD PFTKIEDYNP FNQGQISFIS
EDTETKREVS EYLFEHPVLG KQTWLFDNIA LALEQTDYCD FEIQLEIVHN AIHSWIGGKE
EHSLNHLHYA AYDPIFYLHH SNVDRLWVIW QELQKLRGLN AYESHCALEL MKVPLKPFSF
GAPYNLNDLT TKLSKPEDMF RYKDNFHYEY DILDINSMSI NQIESSYIRH QRDHDRVFAG
FLLSGFGSSA YATFEICIEG GECHEGSHFS VLGGSTEMPW AFDRLYKIEI TDILSDMNLA
FDSAFTIKTK LVAQNGTELP ASILPEATVI RIPPSNEDAD IDTPLNHIRR NVESLDERDI
QNLMAALTRV KEDESDHGFQ TIASYHGSTL CPSPEEPKYA CCLHGMPVFP HWHRVYLLHF
EDSMRRHGSS VATPYWDWTQ PGTKLPRLLA DSDYYDAWTD NVTENPFLRG YIKTEDTYTV
RDVKPELFEI GGGEGSTLYQ QVLLMLEQED YCDFEVQFEV VHNSIHYLVG GHQKYAMSSL
VYSSFDPIFY VHHSMVDRLW AIWQALQEHR HLPFDKAYCA LEQLSFPMKP FVWESNPNLH
TRAASTPQHL FDDNKLGYKY DNLEFHGMNI DQLENAIHKQ QNKDRVFASF LLFGIKTSAD
VHLKLCKDET CEDAGVVFIL GGDNEMPWHF DRTYKKDITH VLHQMHIPLE DLYVHGSTIL
LEVEIETVDG KVLDSSSLPA PSMIYVPAKD FKREVHKKTV GDAIIRKNVN SLTPSDIKEL
RDAMAKVQAD TSDNGYQKIA SYHGIPLSCH YENGTAYACC QHGMVTFPNW HRLLTKQMED
ALVAKGSHVG IPYWDWTTTF ANLPVLVTEE KDNSFHHAHI DVANTDTTRS PRAQLFDDPD
KGDKSFFYRQ IALALEQTDF CDFEIQFEIG HNAIHSWVGG SSPYGMSTLH YTSYDPLFYL
HHSNTDRIWS VWQALQKYRG LPYNTANCEI NKLVKPLKPF NLDTNPNAVT KAHSTGATSF
DYHKLGYDYD NLNFHGMTIP ELEEHLKEIQ HEDRVFAGFL LRTIGQSADV NFDVCTKDGE
CTFGGTFCIL GGEHEMFWAF DRPFKYDITT SLKHLRLDAH DDFDIKVTIK GIDGHVLSNK
YLSPPTVFLA PAKTTH
