UBA1_SCHPO
ID UBA1_SCHPO Reviewed; 1012 AA.
AC O94609; Q9P7R2; Q9USY9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Ubiquitin-activating enzyme E1 1;
DE EC=6.2.1.45 {ECO:0000269|PubMed:23416107};
DE AltName: Full=Poly(A)+ RNA transport protein 3;
GN Name=ptr3; ORFNames=SPBC1604.21c, SPBC211.09;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=9168469; DOI=10.1091/mbc.8.5.825;
RA Azad A.K., Tani T., Shiki N., Tsuneyoshi S., Urushiyama S., Ohshima Y.;
RT "Isolation and molecular characterization of mRNA transport mutants in
RT Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 8:825-841(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3] {ECO:0007744|PDB:4II2, ECO:0007744|PDB:4II3}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 13-1012 IN COMPLEX WITH ATP;
RP UBIQUITIN AND UBC4, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND
RP MUTAGENESIS OF ILE-592; PHE-598; PHE-689 AND PHE-701.
RX PubMed=23416107; DOI=10.1016/j.molcel.2013.01.013;
RA Olsen S.K., Lima C.D.;
RT "Structure of a ubiquitin E1-E2 complex: insights to E1-E2 thioester
RT transfer.";
RL Mol. Cell 49:884-896(2013).
CC -!- FUNCTION: Catalyzes the first step in ubiquitin conjugation to mark
CC cellular proteins for degradation through the ubiquitin-proteasome
CC system. Activates ubiquitin by first adenylating its C-terminal glycine
CC residue with ATP, and thereafter linking this residue to the side chain
CC of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free
CC AMP. {ECO:0000269|PubMed:23416107}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000269|PubMed:23416107};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:23416107}.
CC -!- SUBUNIT: Monomer. Interacts with the E2 ubiquitin-conjugating enzyme
CC ubc4. {ECO:0000269|PubMed:23416107}.
CC -!- INTERACTION:
CC O94609; P0C014; NbExp=2; IntAct=EBI-15837011, EBI-15837044;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: There are two active sites within the E1 molecule,
CC allowing it to accommodate two ubiquitin moieties at a time, with a new
CC ubiquitin forming an adenylate intermediate as the previous one is
CC transferred to the thiol site. {ECO:0000250|UniProtKB:P22515}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
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DR EMBL; D87259; BAA75198.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA22354.1; -; Genomic_DNA.
DR PIR; T50344; T50344.
DR PIR; T52000; T52000.
DR RefSeq; XP_001713148.1; XM_001713096.2.
DR PDB; 4II2; X-ray; 2.20 A; A=13-1012.
DR PDB; 4II3; X-ray; 2.90 A; A/C=13-1012.
DR PDB; 5KNL; X-ray; 2.50 A; A/D=13-1012.
DR PDB; 5UM6; X-ray; 2.79 A; A=13-1012.
DR PDB; 6O82; X-ray; 2.60 A; A/C=13-1012.
DR PDB; 6O83; X-ray; 3.15 A; A/C=13-1012.
DR PDBsum; 4II2; -.
DR PDBsum; 4II3; -.
DR PDBsum; 5KNL; -.
DR PDBsum; 5UM6; -.
DR PDBsum; 6O82; -.
DR PDBsum; 6O83; -.
DR AlphaFoldDB; O94609; -.
DR SMR; O94609; -.
DR BioGRID; 277267; 12.
DR DIP; DIP-48686N; -.
DR IntAct; O94609; 1.
DR STRING; 4896.SPBC1604.21c.1; -.
DR iPTMnet; O94609; -.
DR MaxQB; O94609; -.
DR PaxDb; O94609; -.
DR PRIDE; O94609; -.
DR EnsemblFungi; SPBC1604.21c.1; SPBC1604.21c.1:pep; SPBC1604.21c.
DR PomBase; SPBC1604.21c; ptr3.
DR VEuPathDB; FungiDB:SPBC1604.21c; -.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR InParanoid; O94609; -.
DR OMA; GANLHAF; -.
DR PhylomeDB; O94609; -.
DR Reactome; R-SPO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:O94609; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IDA:PomBase.
DR GO; GO:0000287; F:magnesium ion binding; IDA:PomBase.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IDA:PomBase.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0032446; P:protein modification by small protein conjugation; ISM:PomBase.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.10.2660; -; 1.
DR Gene3D; 2.40.30.180; -; 1.
DR Gene3D; 3.10.290.60; -; 1.
DR Gene3D; 3.50.50.80; -; 1.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR032418; E1_FCCH.
DR InterPro; IPR042302; E1_FCCH_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR018965; Ub-activating_enz_E1_C.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR038252; UBA_E1_C_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR018075; UBQ-activ_enz_E1.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_e1_thiolCys; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; SSF69572; 2.
DR TIGRFAMs; TIGR01408; Ube1; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..1012
FT /note="Ubiquitin-activating enzyme E1 1"
FT /id="PRO_0000194976"
FT ACT_SITE 593
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23416107,
FT ECO:0007744|PDB:4II2, ECO:0007744|PDB:4II3"
FT BINDING 437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23416107,
FT ECO:0007744|PDB:4II2, ECO:0007744|PDB:4II3"
FT BINDING 463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23416107,
FT ECO:0007744|PDB:4II2, ECO:0007744|PDB:4II3"
FT BINDING 474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23416107,
FT ECO:0007744|PDB:4II2"
FT BINDING 487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23416107,
FT ECO:0007744|PDB:4II2, ECO:0007744|PDB:4II3"
FT BINDING 513
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23416107,
FT ECO:0007744|PDB:4II2, ECO:0007744|PDB:4II3"
FT BINDING 537..538
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:23416107,
FT ECO:0007744|PDB:4II2, ECO:0007744|PDB:4II3"
FT MUTAGEN 592
FT /note="I->G: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:23416107"
FT MUTAGEN 598
FT /note="F->A: Nearly abolishes enzyme activity; when
FT associated with A-701."
FT /evidence="ECO:0000269|PubMed:23416107"
FT MUTAGEN 689
FT /note="F->A: Abolishes enzyme activity; when associated
FT with A-701."
FT /evidence="ECO:0000269|PubMed:23416107"
FT MUTAGEN 701
FT /note="F->A: Nearly abolishes enzyme activity; when
FT associated with A-598. Abolishes enzyme activity; when
FT associated with A-689."
FT /evidence="ECO:0000269|PubMed:23416107"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6O83"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:6O82"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 287..304
FT /evidence="ECO:0007829|PDB:4II2"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 315..331
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 340..348
FT /evidence="ECO:0007829|PDB:4II2"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 355..372
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 400..403
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 419..426
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 437..449
FT /evidence="ECO:0007829|PDB:4II2"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:4II3"
FT STRAND 458..462
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:4II2"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 487..498
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 505..509
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:4II2"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 523..527
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 539..552
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 556..562
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 565..571
FT /evidence="ECO:0007829|PDB:4II2"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 579..581
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 592..597
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 602..617
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 619..627
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 633..637
FT /evidence="ECO:0007829|PDB:4II2"
FT TURN 638..640
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 644..655
FT /evidence="ECO:0007829|PDB:4II2"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 663..678
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 680..688
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 698..702
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 704..706
FT /evidence="ECO:0007829|PDB:6O83"
FT HELIX 719..735
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 744..752
FT /evidence="ECO:0007829|PDB:4II2"
FT TURN 780..782
FT /evidence="ECO:0007829|PDB:4II3"
FT HELIX 788..792
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 797..799
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 815..818
FT /evidence="ECO:0007829|PDB:6O83"
FT HELIX 819..833
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 841..848
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 851..853
FT /evidence="ECO:0007829|PDB:6O83"
FT HELIX 856..874
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 880..882
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 885..889
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 890..892
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 894..898
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 905..908
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 911..914
FT /evidence="ECO:0007829|PDB:4II2"
FT TURN 915..917
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 919..924
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 927..936
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 941..947
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 950..954
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 959..963
FT /evidence="ECO:0007829|PDB:4II2"
FT TURN 964..967
FT /evidence="ECO:0007829|PDB:4II2"
FT HELIX 970..977
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 988..996
FT /evidence="ECO:0007829|PDB:4II2"
FT STRAND 1000..1004
FT /evidence="ECO:0007829|PDB:5KNL"
FT STRAND 1007..1011
FT /evidence="ECO:0007829|PDB:4II2"
SQ SEQUENCE 1012 AA; 112949 MW; AB5207808ACC6C2D CRC64;
MSNNMNIDQT DQNTIDEGLY SRQLYVLGHE AMKQMSQSNV LIIGCKGLGV EIAKNVCLAG
VKSVTLYDPQ PTRIEDLSSQ YFLTEDDIGV PRAKVTVSKL AELNQYVPVS VVDELSTEYL
KNFKCVVVTE TSLTKQLEIN DFTHKNHIAY IAADSRGLFG SIFCDFGENF ICTDTDGNEP
LTGMIASITD DGVVTMLEET RHGLENGDFV KFTEVKGMPG LNDGTPRKVE VKGPYTFSIG
SVKDLGSAGY NGVFTQVKVP TKISFKSLRE SLKDPEYVYP DFGKMMRPPQ YHIAFQALSA
FADAHEGSLP RPRNDIDAAE FFEFCKKIAS TLQFDVELDE KLIKEISYQA RGDLVAMSAF
LGGAVAQEVL KATTSKFYPL KQYFYFDSLE SLPSSVTISE ETCKPRGCRY DGQIAVFGSE
FQEKIASLST FLVGAGAIGC EMLKNWAMMG VATGESGHIS VTDMDSIEKS NLNRQFLFRP
RDVGKLKSEC ASTAVSIMNP SLTGKITSYQ ERVGPESEGI FGDEFFEKLS LVTNALDNVE
ARMYVDRRCV FFEKPLLESG TLGTKGNTQV VVPHLTESYG SSQDPPEKSF PICTLKNFPN
RIEHTIAWAR DLFEGLFKQP IDNVNMYLSS PNFLETSLKT SSNPREVLEN IRDYLVTEKP
LSFEECIMWA RLQFDKFFNN NIQQLLFNFP KDSVTSTGQP FWSGPKRAPT PLSFDIHNRE
HFDFIVAAAS LYAFNYGLKS ETDPAIYERV LAGYNPPPFA PKSGIKIQVN ENEEAPETAA
NKDKQELKSI ADSLPPPSSL VGFRLTPAEF EKDDDSNHHI DFITAASNLR AMNYDITPAD
RFKTKFVAGK IVPAMCTSTA VVSGLVCLEL VKLVDGKKKI EEYKNGFFNL AIGLFTFSDP
IASPKMKVNG KEIDKIWDRY NLPDCTLQEL IDYFQKEEGL EVTMLSSGVS LLYANFQPPK
KLAERLPLKI SELVEQITKK KLEPFRKHLV LEICCDDANG EDVEVPFICI KL
