ID   CO5_RAT                 Reviewed;        1681 AA.
AC   P08650; A0A096P6L9; Q63078;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 3.
DT   24-JAN-2024, entry version 145.
DE   RecName: Full=Complement C5;
DE   Contains:
DE     RecName: Full=Complement C5 beta chain;
DE   Contains:
DE     RecName: Full=Complement C5 alpha chain;
DE   Contains:
DE     RecName: Full=C5a anaphylatoxin;
DE   Contains:
DE     RecName: Full=Complement C5 alpha' chain;
DE   Flags: Precursor;
GN   Name=C5;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 679-755.
RC   STRAIN=Lewis; TISSUE=Liver;
RX   PubMed=9116048; DOI=10.1016/s0167-4781(97)00006-7;
RA   Rothermel E., Rolf O., Goetze O., Zwirner J.;
RT   "Nucleotide and corrected amino acid sequence of the functional recombinant
RT   rat anaphylatoxin C5a.";
RL   Biochim. Biophys. Acta 1351:9-12(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 679-755.
RA   Cui L.-X., Ferreri K., Hugli T.E.;
RT   "Characterization of rat C5a, a uniquely active spasmogen.";
RL   Complement 2:18-19(1985).
RN   [4]
RP   PROTEIN SEQUENCE OF 679-755, AND SUBCELLULAR LOCATION.
RC   TISSUE=Serum;
RX   PubMed=7987212; DOI=10.1002/pro.5560030803;
RA   Cui L.-X., Carney D.F., Hugli T.E.;
RT   "Primary structure and functional characterization of rat C5a: an
RT   anaphylatoxin with unusually high potency.";
RL   Protein Sci. 3:1169-1177(1994).
RN   [5] {ECO:0007744|PDB:6JV7, ECO:0007744|PDB:6JV8}
RP   X-RAY CRYSTALLOGRAPHY (1.31 ANGSTROMS) OF 679-749, AND DISULFIDE BONDS.
RA   Zuo C.;
RT   "Chimeric protein probes for C5a receptors through fusion of anaphylatoxin
RT   C5a core region with a small-molecule antagonist.";
RL   Submitted (APR-2019) to the PDB data bank.
CC   -!- FUNCTION: Activation of C5 by a C5 convertase initiates the spontaneous
CC       assembly of the late complement components, C5-C9, into the membrane
CC       attack complex. C5b has a transient binding site for C6. The C5b-C6
CC       complex is the foundation upon which the lytic complex is assembled.
CC   -!- FUNCTION: [C5a anaphylatoxin]: Derived from proteolytic degradation of
CC       complement C5, C5a anaphylatoxin is a mediator of local inflammatory
CC       process. Binding to the receptor C5AR1 induces a variety of responses
CC       including intracellular calcium release, contraction of smooth muscle,
CC       increased vascular permeability, and histamine release from mast cells
CC       and basophilic leukocytes. C5a is also a potent chemokine which
CC       stimulates the locomotion of polymorphonuclear leukocytes and directs
CC       their migration toward sites of inflammation.
CC       {ECO:0000250|UniProtKB:P01031}.
CC   -!- SUBUNIT: C5 precursor is first processed by the removal of 4 basic
CC       residues, forming two chains, beta and alpha, linked by a disulfide
CC       bond. C5 convertase activates C5 by cleaving the alpha chain, releasing
CC       C5a anaphylatoxin and generating C5b (beta chain + alpha' chain).
CC       {ECO:0000250|UniProtKB:P01031}.
CC   -!- SUBUNIT: [C5a anaphylatoxin]: Interacts with C5AR1.
CC       {ECO:0000250|UniProtKB:P01031}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7987212}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AABR07051491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07051499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07051492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07051493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07051494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07051495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07051496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07051497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07051498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07051500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X91892; CAA62994.1; -; mRNA.
DR   PIR; A57689; A57689.
DR   PDB; 6JV7; X-ray; 1.31 A; A=679-749.
DR   PDB; 6JV8; X-ray; 1.58 A; A=680-755.
DR   PDBsum; 6JV7; -.
DR   PDBsum; 6JV8; -.
DR   AlphaFoldDB; P08650; -.
DR   SMR; P08650; -.
DR   STRING; 10116.ENSRNOP00000025534; -.
DR   GlyCosmos; P08650; 6 sites, No reported glycans.
DR   GlyGen; P08650; 6 sites.
DR   PaxDb; 10116-ENSRNOP00000025534; -.
DR   UCSC; RGD:2237; rat.
DR   AGR; RGD:2237; -.
DR   RGD; 2237; C5.
DR   VEuPathDB; HostDB:ENSRNOG00000018899; -.
DR   eggNOG; KOG1366; Eukaryota.
DR   HOGENOM; CLU_001634_4_2_1; -.
DR   InParanoid; P08650; -.
DR   PRO; PR:P08650; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000018899; Expressed in liver and 4 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0005579; C:membrane attack complex; ISO:RGD.
DR   GO; GO:0031714; F:C5a anaphylatoxin chemotactic receptor binding; IDA:RGD.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IDA:RGD.
DR   GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0032835; P:glomerulus development; ISO:RGD.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0090594; P:inflammatory response to wounding; ISO:RGD.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IDA:RGD.
DR   GO; GO:0001822; P:kidney development; ISO:RGD.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IMP:RGD.
DR   GO; GO:0033602; P:negative regulation of dopamine secretion; IDA:RGD.
DR   GO; GO:0010760; P:negative regulation of macrophage chemotaxis; ISO:RGD.
DR   GO; GO:0010700; P:negative regulation of norepinephrine secretion; IDA:RGD.
DR   GO; GO:0001780; P:neutrophil homeostasis; ISO:RGD.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR   GO; GO:0032722; P:positive regulation of chemokine production; ISO:RGD.
DR   GO; GO:0050921; P:positive regulation of chemotaxis; IDA:RGD.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR   GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:RGD.
DR   CDD; cd00017; ANATO; 1.
DR   CDD; cd02896; complement_C3_C4_C5; 1.
DR   Gene3D; 1.50.10.20; -; 1.
DR   Gene3D; 2.20.130.20; -; 1.
DR   Gene3D; 2.40.50.120; -; 1.
DR   Gene3D; 2.60.120.1540; -; 1.
DR   Gene3D; 2.60.40.1930; -; 3.
DR   Gene3D; 2.60.40.1940; -; 1.
DR   Gene3D; 6.20.50.160; -; 1.
DR   Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR   Gene3D; 1.20.91.20; Anaphylotoxins (complement system); 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR   InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR011626; Alpha-macroglobulin_TED.
DR   InterPro; IPR000020; Anaphylatoxin/fibulin.
DR   InterPro; IPR018081; Anaphylatoxin_comp_syst.
DR   InterPro; IPR041425; C3/4/5_MG1.
DR   InterPro; IPR048843; C5_CUB.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR001599; Macroglobln_a2.
DR   InterPro; IPR002890; MG2.
DR   InterPro; IPR041555; MG3.
DR   InterPro; IPR040839; MG4.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR018933; Netrin_module_non-TIMP.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   PANTHER; PTHR11412:SF83; COMPLEMENT C5; 1.
DR   PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR   Pfam; PF00207; A2M; 1.
DR   Pfam; PF07703; A2M_BRD; 1.
DR   Pfam; PF07677; A2M_recep; 1.
DR   Pfam; PF01821; ANATO; 1.
DR   Pfam; PF21309; C5_CUB; 1.
DR   Pfam; PF17790; MG1; 1.
DR   Pfam; PF01835; MG2; 1.
DR   Pfam; PF17791; MG3; 1.
DR   Pfam; PF17789; MG4; 1.
DR   Pfam; PF01759; NTR; 1.
DR   Pfam; PF07678; TED_complement; 1.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01359; A2M_N_2; 1.
DR   SMART; SM01361; A2M_recep; 1.
DR   SMART; SM00104; ANATO; 1.
DR   SMART; SM00643; C345C; 1.
DR   SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR   SUPFAM; SSF47686; Anaphylotoxins (complement system); 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR   SUPFAM; SSF50242; TIMP-like; 1.
DR   PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR   PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR   PROSITE; PS50189; NTR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cleavage on pair of basic residues;
KW   Complement alternate pathway; Complement pathway; Cytolysis;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW   Inflammatory response; Innate immunity; Membrane attack complex;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..674
FT                   /note="Complement C5 beta chain"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000453364"
FT   PROPEP          675..678
FT                   /evidence="ECO:0000250|UniProtKB:P01031"
FT                   /id="PRO_0000453365"
FT   CHAIN           679..1681
FT                   /note="Complement C5 alpha chain"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000453366"
FT   CHAIN           679..755
FT                   /note="C5a anaphylatoxin"
FT                   /evidence="ECO:0000269|PubMed:7987212, ECO:0000269|Ref.3"
FT                   /id="PRO_0000005996"
FT   CHAIN           756..1681
FT                   /note="Complement C5 alpha' chain"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000453367"
FT   DOMAIN          702..736
FT                   /note="Anaphylatoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT   DOMAIN          1536..1680
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   REGION          696..725
FT                   /note="Involved in C5AR1 binding"
FT                   /evidence="ECO:0000250|UniProtKB:P01031"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        915
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1634
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        567..814
FT                   /evidence="ECO:0000250|UniProtKB:P01031"
FT   DISULFID        635..670
FT                   /evidence="ECO:0000250|UniProtKB:P01031"
FT   DISULFID        702..728
FT                   /evidence="ECO:0007744|PDB:6JV7, ECO:0007744|PDB:6JV8"
FT   DISULFID        703..735
FT                   /evidence="ECO:0007744|PDB:6JV7, ECO:0007744|PDB:6JV8"
FT   DISULFID        715..736
FT                   /evidence="ECO:0007744|PDB:6JV7, ECO:0007744|PDB:6JV8"
FT   DISULFID        860..887
FT                   /evidence="ECO:0000250|UniProtKB:P01031"
FT   DISULFID        870..1531
FT                   /evidence="ECO:0000250|UniProtKB:P01031"
FT   DISULFID        1105..1163
FT                   /evidence="ECO:0000250|UniProtKB:P01031"
FT   DISULFID        1379..1509
FT                   /evidence="ECO:0000250|UniProtKB:P01031"
FT   DISULFID        1409..1478
FT                   /evidence="ECO:0000250|UniProtKB:P01031"
FT   DISULFID        1524..1529
FT                   /evidence="ECO:0000250|UniProtKB:P01031"
FT   DISULFID        1536..1610
FT                   /evidence="ECO:0000250|UniProtKB:P01031"
FT   DISULFID        1557..1680
FT                   /evidence="ECO:0000250|UniProtKB:P01031"
FT   DISULFID        1658..1661
FT                   /evidence="ECO:0000250|UniProtKB:P01031"
FT   CONFLICT        733
FT                   /note="N -> K (in Ref. 3; AA sequence and 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        739..741
FT                   /note="ADK -> DP (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        741
FT                   /note="K -> H (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        745..747
FT                   /note="ESH -> NES (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        745..747
FT                   /note="ESH -> NQS (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           683..691
FT                   /evidence="ECO:0007829|PDB:6JV7"
FT   HELIX           697..707
FT                   /evidence="ECO:0007829|PDB:6JV7"
FT   HELIX           715..719
FT                   /evidence="ECO:0007829|PDB:6JV7"
FT   HELIX           726..749
FT                   /evidence="ECO:0007829|PDB:6JV7"
SQ   SEQUENCE   1681 AA;  189081 MW;  56D466A91F0D153C CRC64;
     MGLWGLLCLL IFLDKTWGQE QTYVISAPKI FRVGSSENVV IQAHGYTEAF DATISLKSYP
     DKKVTYSSGY VNLSPENKFQ NSALLTLPPK QFPRDENPVS HVYLEVVSMH FSKSKKIPIT
     YDNGFLFIHT DKPVYTPDQS VKIRVYSLSD DLKPAKRETV LTFVDPEGTE VDIVEENDYT
     GIISFPDFKI PSNPKYGVWT IKAKYKKDFT TTGTAYFEVK EYVLPRFSVS IEPESNFIGY
     KNFKNFEITV KARYFYNKMV PDAEVYIFFG LREDIKEDEK QMMHKAMQAA TLMDGAAQTC
     WLAETEVREI NYNMFEDRNN NYSYIACTVT ESSGGFSEEA EIPGIKYVLS PYTLNLVATP
     LFLKPGIPFS IKVQVKDSLE QLVGGVPVTL MAQTVNVNQE TSDLEPKRSI THSADGVASF
     VVNLPSEVTS LKFEVKTDAP ELPEENQASK EYEAVTYSSL SQSYIYIGWT ENYKPMLVGE
     YLNIIVTPKS PYIDKITHYN YLILSKGKIV QYGTKEKLLY SSYQNINIPV TQDMVPSARL
     LVYYIVTGEQ TAELVADAVW INIEEKCGNQ LQVHLSPDKD VYSPGQTVSL DMVTEADSWV
     ALSAVDSAVY GVRGKAKRAM QRVFQAFDDK SDLGCGAGGG RDNVDVFHLA GLTFLTNANA
     DDSQYHDDSC KEILRPKRDL QLLHQKVEEQ AAKYKHRVPK KCCYDGAREN KYETCEQRVA
     RVTIGPHCIR AFNECCTIAD KIRKESHHKG MLLGRIQIKA LLPVMKAEIR SYFPESWLWE
     VHRVPKRNQL QVALPDSLTT WEIQGIGISD NGICVADTLK AKVFKDVFLE MNIPYSVVRG
     EQIQLKGTVY NYRTSGTMFC VKMSAVEGIC TPGSSAASPQ TSRSSRCVRQ RIEGSSSHLV
     TFSLLPLEIG LHSINFSLET SFGKEILVKT LRVVPEGIKR ESYAGVTLDP RGVYGIVNRR
     KEFPYRIPLD LVPKTNVKRI LSVKGLLIGE FLSTVLSKEG IDILTHLPKG SAEAELMSIV
     PVFYVFHYLE AGNHWNIFHP DTLARKQSLQ KKIKEGLVSV MSYRNADYSY SMWKGASSSA
     WLTAFALRVL GQVNKYVKQD QYSICNSLLW LIEKCQLENG SFKENSQYLP IKLQGTLPAE
     AQENTLYLTA FSVIGIRKAI GICPTEKIYT ALAKADSFLL ERTLPSKSTF TLAIVAYALS
     LGDRTHPKFR SIVSALKREA LVKGDPPIYR FWRDTLQRPD SSAPNSGTAG MVETTAYALL
     TSLNLKETSY VNPIIKWLSE EQRYGGGFYS TQDTINAIEG LTEYSLLVKQ LHLDMDINVS
     YKHKGDFYQY KVTEKNFLGR PVEVPLNDDL IVTTGYSSGL ATVYVKTVVH KTSVAEEFCS
     FYLKIDTQEV EASSYLSYSD SGHKRIIACA SYKPSKEESA SGSSHAVMDI LLPTGIGANQ
     EDLRALVEGV DQLLTDYQIK DSHVILQLNS IPSRDFLCVR FRIFELFQVG FLNPATFTVY
     EYHRPDKQCT MIYSTSDTNL QRVCEGAACK CVEADCGQLQ AELDLAISAD TRKETACKPE
     IAYAYKVRIT SATEENIFVK YTATLLDIYK TGEAAAEKDS EITFIKKISC TNANLVKGKQ
     YLIMGKEALQ IKHNFSFKYI YPLDSSTWIE YWPTDTTCPS CQAFVANLDE FAEDIFLNGC
     E
//