MPRI_BOVIN
ID MPRI_BOVIN Reviewed; 2499 AA.
AC P08169;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 25-MAY-2022, entry version 168.
DE RecName: Full=Cation-independent mannose-6-phosphate receptor;
DE Short=CI Man-6-P receptor;
DE Short=CI-MPR;
DE Short=M6PR;
DE AltName: Full=300 kDa mannose 6-phosphate receptor;
DE Short=MPR 300;
DE AltName: Full=Insulin-like growth factor 2 receptor;
DE AltName: Full=Insulin-like growth factor II receptor;
DE Short=IGF-II receptor;
DE AltName: CD_antigen=CD222;
DE Flags: Precursor;
GN Name=IGF2R; Synonyms=M6P;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2963004; DOI=10.1016/s0021-9258(18)69244-0;
RA Lobel P., Dahms N.M., Kornfeld S.;
RT "Cloning and sequence analysis of the cation-independent mannose 6-
RT phosphate receptor.";
RL J. Biol. Chem. 263:2563-2570(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Killian J.K.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1039-2499.
RX PubMed=2951738; DOI=10.1073/pnas.84.8.2233;
RA Lobel P., Dahms N.M., Breitmeyer J., Chirgwin J.M., Kornfeld S.;
RT "Cloning of the bovine 215-kDa cation-independent mannose 6-phosphate
RT receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:2233-2237(1987).
RN [4]
RP INTERACTION WITH HA-I AND HA-II ADAPTERS, AND MUTAGENESIS OF
RP 2360-TYR--TYR-2362.
RX PubMed=2545438; DOI=10.1002/j.1460-2075.1989.tb03471.x;
RA Glickman J.N., Conibear E., Pearse B.M.F.;
RT "Specificity of binding of clathrin adapters to signals on the mannose-6-
RT phosphate/insulin-like growth factor II receptor.";
RL EMBO J. 8:1041-1047(1989).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 45-476, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-120 AND ASN-409.
RX PubMed=15085180; DOI=10.1038/sj.emboj.7600215;
RA Olson L.J., Yammani R.D., Dahms N.M., Kim J.J.;
RT "Structure of uPAR, plasminogen, and sugar-binding sites of the 300 kDa
RT mannose 6-phosphate receptor.";
RL EMBO J. 23:2019-2028(2004).
RN [6]
RP STRUCTURE BY NMR OF 628-769, DISULFIDE BONDS, AND MUTAGENESIS OF TYR-723.
RX PubMed=20615935; DOI=10.1073/pnas.1004232107;
RA Olson L.J., Peterson F.C., Castonguay A., Bohnsack R.N., Kudo M.,
RA Gotschall R.R., Canfield W.M., Volkman B.F., Dahms N.M.;
RT "Structural basis for recognition of phosphodiester-containing lysosomal
RT enzymes by the cation-independent mannose 6-phosphate receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12493-12498(2010).
CC -!- FUNCTION: Mediates the transport of phosphorylated lysosomal enzymes
CC from the Golgi complex and the cell surface to lysosomes. Lysosomal
CC enzymes bearing phosphomannosyl residues bind specifically to mannose-
CC 6-phosphate receptors in the Golgi apparatus and the resulting
CC receptor-ligand complex is transported to an acidic prelysosomal
CC compartment where the low pH mediates the dissociation of the complex.
CC The receptor is then recycled back to the Golgi for another round of
CC trafficking through its binding to the retromer. This receptor also
CC binds IGF2. Acts as a positive regulator of T-cell coactivation by
CC binding DPP4. {ECO:0000250|UniProtKB:P11717}.
CC -!- SUBUNIT: Binds HA-I and HA-II plasma membrane adapters
CC (PubMed:2545438). Interacts with DPP4; the interaction is direct. Binds
CC GGA1, GGA2 and GGA3 (By similarity). Interacts with the heterotrimeric
CC retromer cargo-selective complex (CSC), formed by VPS26 (VPS26A or
CC VPS26B), VPS29 and VPS35; which is involved in retrograde trafficking
CC of the receptor from endosomes to the Golgi apparatus (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P11717,
CC ECO:0000269|PubMed:2545438}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P11717}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P11717}. Endosome membrane
CC {ECO:0000250|UniProtKB:P11717}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P11717}. Note=Mainly localized in the Golgi at
CC steady state and not detectable in lysosome. Colocalized with DPP4 in
CC internalized cytoplasmic vesicles adjacent to the cell surface.
CC {ECO:0000250|UniProtKB:P11717}.
CC -!- DOMAIN: Contains 15 repeating units of approximately 147 AA harboring
CC four disulfide bonds each. The most highly conserved region within the
CC repeat consists of a stretch of 13 AA that contains cysteines at both
CC ends.
CC -!- PTM: Palmitoylated. Undergoes cysteine S-palmitoylation which promotes
CC interaction with the retromer cargo-selective complex which mediates
CC its retrograde trafficking to the Golgi apparatus.
CC {ECO:0000250|UniProtKB:P11717}.
CC -!- SIMILARITY: Belongs to the MRL1/IGF2R family. {ECO:0000305}.
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DR EMBL; J03527; AAA30455.1; -; mRNA.
DR EMBL; AF342811; AAL23908.1; -; mRNA.
DR PIR; A25908; A30788.
DR RefSeq; NP_776777.1; NM_174352.2.
DR PDB; 1Q25; X-ray; 1.80 A; A=45-476.
DR PDB; 1SYO; X-ray; 2.20 A; A/B=45-476.
DR PDB; 1SZ0; X-ray; 2.10 A; A/B=45-476.
DR PDB; 2KVA; NMR; -; A=628-769.
DR PDB; 2KVB; NMR; -; A=628-769.
DR PDB; 6UM1; EM; 3.46 A; A=1-2499.
DR PDB; 6UM2; EM; 4.32 A; A=1-2499.
DR PDBsum; 1Q25; -.
DR PDBsum; 1SYO; -.
DR PDBsum; 1SZ0; -.
DR PDBsum; 2KVA; -.
DR PDBsum; 2KVB; -.
DR PDBsum; 6UM1; -.
DR PDBsum; 6UM2; -.
DR AlphaFoldDB; P08169; -.
DR SMR; P08169; -.
DR BioGRID; 159160; 5.
DR ELM; P08169; -.
DR STRING; 9913.ENSBTAP00000037502; -.
DR UniLectin; P08169; -.
DR iPTMnet; P08169; -.
DR PaxDb; P08169; -.
DR PRIDE; P08169; -.
DR GeneID; 281849; -.
DR KEGG; bta:281849; -.
DR CTD; 3482; -.
DR eggNOG; KOG4504; Eukaryota.
DR InParanoid; P08169; -.
DR OrthoDB; 290124at2759; -.
DR EvolutionaryTrace; P08169; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; TAS:AgBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0005520; F:insulin-like growth factor binding; IMP:AgBase.
DR GO; GO:0036143; F:kringle domain binding; IPI:AgBase.
DR GO; GO:0005537; F:mannose binding; IDA:AgBase.
DR GO; GO:0051219; F:phosphoprotein binding; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0007041; P:lysosomal transport; IEA:InterPro.
DR CDD; cd00062; FN2; 1.
DR Gene3D; 2.10.10.10; -; 1.
DR Gene3D; 2.70.130.10; -; 15.
DR InterPro; IPR000479; CIMR_rpt.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR Pfam; PF00878; CIMR; 15.
DR Pfam; PF00040; fn2; 1.
DR SMART; SM00059; FN2; 1.
DR SUPFAM; SSF50911; SSF50911; 15.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS51914; MRH; 15.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disulfide bond; Endosome; Glycoprotein;
KW Golgi apparatus; Lipoprotein; Membrane; Methylation; Palmitate;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..2499
FT /note="Cation-independent mannose-6-phosphate receptor"
FT /id="PRO_0000019228"
FT TOPO_DOM 45..2313
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2314..2336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2337..2499
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 55..169
FT /note="MRH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 178..326
FT /note="MRH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 332..477
FT /note="MRH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 482..628
FT /note="MRH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 634..770
FT /note="MRH 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 773..932
FT /note="MRH 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 940..1088
FT /note="MRH 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 1091..1228
FT /note="MRH 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 1234..1372
FT /note="MRH 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 1376..1517
FT /note="MRH 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 1523..1657
FT /note="MRH 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 1659..1806
FT /note="MRH 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 1811..1998
FT /note="MRH 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 1907..1953
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 2001..2136
FT /note="MRH 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 2144..2289
FT /note="MRH 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 2414..2499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2414..2429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2440..2455
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2456..2476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2361
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11717"
FT MOD_RES 2421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11717"
FT MOD_RES 2438
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q07113"
FT MOD_RES 2492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11717"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15085180"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15085180"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 755
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 959
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1030
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1825
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2094
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 85..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 125..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 140..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 180..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 234..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 281..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 294..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 334..375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 383..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 429..463
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 443..475
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 484..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 540..547
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 581..614
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 595..626
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 636..672
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 680..687
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 739..768
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 775..822
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 831..838
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 883..918
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 901..930
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 942..978
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 984..995
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1051..1086
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1093..1134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1143..1150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1186..1214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1199..1226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1236..1271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1279..1291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1328..1358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1342..1370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1378..1417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1429..1436
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1470..1503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1485..1515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1525..1562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1568..1575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1607..1643
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1623..1655
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1661..1704
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1715..1722
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1759..1792
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1775..1804
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1813..1848
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1859..1865
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1902..1984
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 1912..1936
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 1926..1951
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 1966..1996
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 2003..2038
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 2048..2055
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 2091..2122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 2105..2134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 2197..2203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 2241..2275
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 2257..2287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT MUTAGEN 723
FT /note="Y->F: No noticeable change in Man-6-P and Man-P-
FT GlcNAc recognition."
FT /evidence="ECO:0000269|PubMed:20615935"
FT MUTAGEN 723
FT /note="Y->L: Severely impairs both Man-6-P and Man-P-GlcNAc
FT recognition."
FT /evidence="ECO:0000269|PubMed:20615935"
FT MUTAGEN 2360..2362
FT /note="YKY->AKV: Loss of interaction between HA-II adapters
FT and these tails, but does not affect the interaction
FT between them and HA-I."
FT /evidence="ECO:0000269|PubMed:2545438"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:1Q25"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1Q25"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 154..163
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1SZ0"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 305..319
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 366..372
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:1SZ0"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:1SZ0"
FT STRAND 436..443
FT /evidence="ECO:0007829|PDB:1Q25"
FT TURN 448..452
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 464..471
FT /evidence="ECO:0007829|PDB:1Q25"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:1Q25"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 535..539
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 545..549
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 570..577
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 588..595
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 611..615
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 618..623
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 631..639
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:6UM1"
FT HELIX 650..652
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 658..661
FT /evidence="ECO:0007829|PDB:2KVA"
FT STRAND 663..669
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 671..673
FT /evidence="ECO:0007829|PDB:2KVA"
FT STRAND 684..693
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 696..698
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 701..703
FT /evidence="ECO:0007829|PDB:2KVB"
FT STRAND 706..709
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 712..717
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 733..739
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 748..750
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 753..767
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 802..804
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 815..819
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 821..823
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 836..842
FT /evidence="ECO:0007829|PDB:6UM1"
FT HELIX 869..871
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 873..879
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 894..901
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 917..920
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 923..927
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 937..939
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 942..945
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 947..949
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 952..954
FT /evidence="ECO:0007829|PDB:6UM1"
FT HELIX 956..958
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 964..966
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 968..970
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 973..975
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 977..979
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1019..1021
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1023..1025
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1027..1030
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1032..1034
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1046..1050
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1065..1067
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1070..1072
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1074..1076
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1098..1100
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1102..1104
FT /evidence="ECO:0007829|PDB:6UM1"
FT HELIX 1106..1109
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1133..1135
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1141..1143
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1151..1154
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1175..1180
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1192..1198
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1207..1212
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1215..1220
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1234..1236
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1241..1243
FT /evidence="ECO:0007829|PDB:6UM1"
FT HELIX 1250..1252
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1253..1255
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1257..1260
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1265..1268
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1290..1293
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1311..1314
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1317..1322
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1329..1333
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1335..1344
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1346..1352
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1359..1367
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1378..1381
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1387..1389
FT /evidence="ECO:0007829|PDB:6UM1"
FT HELIX 1391..1393
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1396..1398
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1411..1414
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1416..1419
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1425..1427
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1434..1441
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1444..1449
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1454..1456
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1459..1465
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1473..1475
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1478..1483
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1495..1500
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 1501..1503
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1504..1509
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1520..1527
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 1530..1532
FT /evidence="ECO:0007829|PDB:6UM1"
FT HELIX 1539..1541
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1547..1554
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1556..1559
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1561..1563
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1566..1568
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 1577..1580
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1590..1592
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1597..1599
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1608..1612
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1617..1623
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1626..1628
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1637..1639
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 1640..1643
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1644..1647
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1650..1654
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1662..1665
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1668..1671
FT /evidence="ECO:0007829|PDB:6UM1"
FT HELIX 1673..1675
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1678..1680
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1699..1701
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1703..1705
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1720..1723
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1744..1747
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1749..1754
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1764..1766
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1768..1775
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1791..1800
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1834..1840
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1842..1845
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1847..1849
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 1853..1855
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1856..1858
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1860..1870
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1875..1877
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 1878..1880
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 1887..1890
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1891..1896
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1898..1900
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1907..1909
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1916..1918
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1921..1925
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1929..1933
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1935..1942
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 1943..1945
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1948..1950
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1959..1966
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1977..1981
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1984..1989
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 1992..1996
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2004..2006
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2011..2013
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 2015..2017
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2020..2022
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2037..2039
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2046..2048
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 2050..2052
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2055..2057
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2063..2065
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2074..2077
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2080..2083
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2091..2095
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2110..2117
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2119..2121
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2124..2131
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 2151..2154
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 2160..2162
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2168..2171
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2173..2175
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2178..2180
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2182..2184
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2199..2202
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2209..2211
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2220..2223
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2231..2235
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2237..2239
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2252..2255
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2261..2263
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2270..2272
FT /evidence="ECO:0007829|PDB:6UM1"
FT TURN 2273..2275
FT /evidence="ECO:0007829|PDB:6UM1"
FT STRAND 2276..2281
FT /evidence="ECO:0007829|PDB:6UM1"
SQ SEQUENCE 2499 AA; 274529 MW; 3C1C9DEF2875159D CRC64;
MEAAAGRSSH LGPAPAGRPP RCPLLLQLQL LLLLLLLPPG WVPGAAGTQG AEFPELCSYT
WEAVDTKNNM LYKINICGNM GVAQCGPSSA VCMHDLKTDS FHSVGDSLLK TASRSLLEFN
TTVNCKQQNH KIQSSITFLC GKTLGTPEFV TATDCVHYFE WRTTAACKKN IFKANKEVPC
YAFDRELKKH DLNPLIKTSG AYLVDDSDPD TSLFINVCRD IEVLRASSPQ VRVCPTGAAA
CLVRGDRAFD VGRPQEGLKL VSNDRLVLSY VKEGAGQPDF CDGHSPAVTI TFVCPSERRE
GTIPKLTAKS NCRFEIEWVT EYACHRDYLE SRSCSLSSAQ HDVAVDLQPL SRVEASDSLF
YTSEADEYTY YLSICGGSQA PICNKKDAAV CQVKKADSTQ VKVAGRPQNL TLRYSDGDLT
LIYFGGEECS SGFQRMSVIN FECNQTAGNN GRGAPVFTGE VDCTYFFTWD TKYACVHEKE
ALLCGVSDGK QRFDLSALAR HSELEQNWEA VDGSQREAEK KHFFINICHR VLQTGQARGC
PEDAAVCAVD KNGSKNLGRF ISSPTREKGN IQLSYSDGDE CGGGQKIITN ITLMCKPGDL
ESAPVLTTSR ADGCFYEFEW RTAAACVLSR TEGDNCTVFD SQAGFSFDLT PLTKKDAYKV
ETDKYEFHIN VCGPVSVGAC PPDSGACQVS RSDRKSWNLG RSNAKLSYYD GMIQLTYRDG
TPYNNEKRTP RATLITFLCD RDAGVGFPEY QEEDNSTYNF RWYTSYACPE EPLECIVTDP
VTLDQYDLSR LAKSEGGPGG NWYSLDNGGA RSTWRKYYIN VCRPLNPVPG CDRYASACQM
KYQGEQGSYS ETVSISNLGV AKTGPMVEDS GSLLLEYVNG SACTTSDQRR TTYTTRIHLV
CSTGSLYTHP IFSLNWECVV SFLWNTAAAC PIRITTDIDQ VCSIKDPNSG YVFDLNPLNN
SRGYVVLGIG KTFLFNVCGD MPACGTLDGK PASGCEAEVQ MDDMKTLKPG RLVGLEKSLQ
LSTEGFITLN YTGLPSHPNG RADAFIIRFV CNDDVYPGTP KFLHQDIDSS LGIRDTFFEF
ETALACVPSP VDCQVTDPAG NEYDLSGLSK ARKPWTAVDT FDEGKKRTFY LSVCTPLPYI
PGCHGTAVGC CLVTEDSKLN LGVVQISPQV GANGSLSLVY VNGDKCKNQR FSTRINLECA
HTTGSPTFQL QNDCEYVFLW RTVEACPVVR AEGDYCEVRD PRHGNLYNLI PLGLNDTVVR
AGEYTYYFRV CGELTSGVCP TSDKSKVISS CQEKRGPQGF QKVAGLFNQK LTYENGVLKM
NYTGGDTCHK VYQRSTTIFF YCDRSTQAPV FLQETSDCSY LFEWRTQYAC PPYDLTECSF
KNEAGETYDL SSLSRYSDNW EAVTGTGSTE HYLINVCKSL SPQAGSDPCP PEAAVCLLGG
PKPVNLGRVR DSPQWSQGLT LLKYVDGDLC PDQIRKKSTT IRFTCSESHV NSRPMFISAV
EDCEYTFSWP TAAACAVKSN VHDDCQVTNP ATGHLFDLSS LSGRAGFTAA YSEKGLVYLS
VCGDNENCAN GVGACFGQTR ISVGKASKRL TYVDQVLQLV YEGGSPCPSK TGLSYKSVIS
FVCRPEVGPT NRPMLISLDK RTCTLFFSWH TPLACEQTTE CSVRNGSSLI DLSPLIHRTG
GYEAYDESED DGSDTSPDFY INICQPLNPM HGLACPAGTA VCKVPVDGPP IDIGRVAGPP
ILNPIANEVY LNFESSTPCL ADRHFNYTSL ITFHCKRGVS MGTPKLLRTS VCDFVFEWET
PLVCPDEVKT DGCSLTDEQL YYSFNLSSLS KSTFKVTRGP HTYSVGVCTA AAGLDEGGCK
DGAVCLLSGS KGASFGRLAS MKLDYRHQDE AVILSYANGD TCPPETEDGE PCVFPFVFNG
KSYEECVVES RARLWCATTA NYDRDHEWGF CKHSTSHRTS VIIFKCDEDA DVGRPQVFSE
VRGCEVTFEW KTKVVCPPKK MECKFVQKHR TYDLRLLSSL TGSWSFVHNG ASYYINLCQK
IYKGPQDCSE RASVCKKSTS GEVQVLGLVH TQKLDVVDDR VIVTYSKGHY CGDNKTASAV
IELTCAKTVG RPSFTRFDVD SCTYHFSWDS RAACAVKPQE VQMVNGTITN PANGRSFSLG
DIYFKRFSAS GDVRTNGDRY IYEIQLSSIT GSSSPACSGA SICQRKANDQ HFSRKVGTSN
QTRYYVQDGD LDVVFTSSSK CGKDKTKSVS STIFFHCDPL VKDGIPEFSH ETADCQYLFS
WHTSAVCPLG AGFDEEIAGD DAQEHKGLSE RSQAVGAVLS LLLVALTACL LTLLLYKKER
REMVMSRLTN CCRRSANVSY KYSKVNKEEE ADENETEWLM EEIQPPAPRP GKEGQENGHV
AAKSVRAADT LSALHGDEQD SEDEVLTLPE VKVRPPGRAP GAEGGPPLRP LPRKAPPPLR
ADDRVGLVRG EPARRGRPRA AATPISTFHD DSDEDLLHV
