TLL1_HUMAN
ID TLL1_HUMAN Reviewed; 1013 AA.
AC O43897; B2RMU2; Q96AN3; Q9NQS4;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Tolloid-like protein 1;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=TLL1; Synonyms=TLL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Greenspan D.S., Takahara K.;
RT "Sequence of human mammalian tolloid-like (mTll) and chromosomal
RT localization of the cognate gene TLL.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RA Arleth A.J., Elshourbagy N.A., Li X., Willette R.N.;
RT "Human cardiac/brain tolloid-like protein.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP CHARACTERIZATION OF ACTION ON COLLAGENS.
RX PubMed=10479448; DOI=10.1006/dbio.1999.9383;
RA Scott I.C., Blitz I.L., Pappano W.N., Imamura Y., Clark T.G.,
RA Steiglitz B.M., Thomas C.L., Maas S.A., Takahara K., Cho K.W.,
RA Greenspan D.S.;
RT "Mammalian BMP-1/Tolloid-related metalloproteinases, including novel family
RT member mammalian Tolloid-like 2, have differential enzymatic activities and
RT distributions of expression relevant to patterning and skeletogenesis.";
RL Dev. Biol. 213:283-300(1999).
RN [6]
RP CHARACTERIZATION OF ACTION ON PROBIGLYCAN.
RX PubMed=10896944; DOI=10.1074/jbc.m004846200;
RA Scott I.C., Imamura Y., Pappano W.N., Troedel J.M., Recklies A.D.,
RA Roughley P.J., Greenspan D.S.;
RT "Bone morphogenetic protein-1 processes probiglycan.";
RL J. Biol. Chem. 275:30504-30511(2000).
RN [7]
RP CHARACTERIZATION OF ACTION ON PRO-LYSYL OXIDASE.
RX PubMed=11313359; DOI=10.1074/jbc.m102352200;
RA Uzel M.I., Scott I.C., Babakhanlou-Chase H., Palamakumbura A.H.,
RA Pappano W.N., Hong H.-H., Greenspan D.S., Trackman P.C.;
RT "Multiple bone morphogenetic protein 1-related mammalian metalloproteinases
RT process pro-lysyl oxidase at the correct physiological site and control
RT lysyl oxidase activation in mouse embryo fibroblast cultures.";
RL J. Biol. Chem. 276:22537-22543(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 148-348, AND DISULFIDE BONDS.
RX PubMed=18824173; DOI=10.1016/j.jmb.2008.09.029;
RA Mac Sweeney A., Gil-Parrado S., Vinzenz D., Bernardi A., Hein A.,
RA Bodendorf U., Erbel P., Logel C., Gerhartz B.;
RT "Structural basis for the substrate specificity of bone morphogenetic
RT protein 1/tolloid-like metalloproteases.";
RL J. Mol. Biol. 384:228-239(2008).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-688.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [10]
RP VARIANTS ASD6 LEU-182; ALA-238 AND VAL-629.
RX PubMed=18830233; DOI=10.1038/ejhg.2008.175;
RA Stanczak P., Witecka J., Szydlo A., Gutmajster E., Lisik M.,
RA Augusciak-Duma A., Tarnowski M., Czekaj T., Czekaj H., Sieron A.L.;
RT "Mutations in mammalian tolloid-like 1 gene detected in adult patients with
RT ASD.";
RL Eur. J. Hum. Genet. 17:344-351(2009).
CC -!- FUNCTION: Protease which processes procollagen C-propeptides, such as
CC chordin, pro-biglycan and pro-lysyl oxidase. Required for the embryonic
CC development. Predominant protease, which in the development, influences
CC dorsal-ventral patterning and skeletogenesis.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU01211};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43897-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43897-2; Sequence=VSP_017197, VSP_017198;
CC -!- DISEASE: Atrial septal defect 6 (ASD6) [MIM:613087]: A congenital heart
CC malformation characterized by incomplete closure of the wall between
CC the atria resulting in blood flow from the left to the right atria.
CC {ECO:0000269|PubMed:18830233}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; U91963; AAB93878.1; -; mRNA.
DR EMBL; AF282732; AAF86287.1; -; mRNA.
DR EMBL; CH471056; EAX04813.1; -; Genomic_DNA.
DR EMBL; BC016922; AAH16922.1; -; mRNA.
DR EMBL; BC136429; AAI36430.1; -; mRNA.
DR EMBL; BC136430; AAI36431.1; -; mRNA.
DR CCDS; CCDS3811.1; -. [O43897-1]
DR CCDS; CCDS56342.1; -. [O43897-2]
DR RefSeq; NP_001191689.1; NM_001204760.1. [O43897-2]
DR RefSeq; NP_036596.3; NM_012464.4. [O43897-1]
DR PDB; 3EDI; X-ray; 1.40 A; A=148-348.
DR PDBsum; 3EDI; -.
DR AlphaFoldDB; O43897; -.
DR SMR; O43897; -.
DR BioGRID; 112947; 5.
DR IntAct; O43897; 5.
DR STRING; 9606.ENSP00000061240; -.
DR BindingDB; O43897; -.
DR ChEMBL; CHEMBL4295664; -.
DR MEROPS; M12.016; -.
DR GlyConnect; 1819; 1 N-Linked glycan (1 site).
DR GlyGen; O43897; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; O43897; -.
DR PhosphoSitePlus; O43897; -.
DR BioMuta; TLL1; -.
DR MassIVE; O43897; -.
DR MaxQB; O43897; -.
DR PaxDb; O43897; -.
DR PeptideAtlas; O43897; -.
DR PRIDE; O43897; -.
DR ProteomicsDB; 49221; -. [O43897-1]
DR ProteomicsDB; 49222; -. [O43897-2]
DR Antibodypedia; 28327; 120 antibodies from 20 providers.
DR DNASU; 7092; -.
DR Ensembl; ENST00000061240.7; ENSP00000061240.2; ENSG00000038295.8. [O43897-1]
DR Ensembl; ENST00000513213.5; ENSP00000422937.1; ENSG00000038295.8. [O43897-2]
DR GeneID; 7092; -.
DR KEGG; hsa:7092; -.
DR MANE-Select; ENST00000061240.7; ENSP00000061240.2; NM_012464.5; NP_036596.3.
DR UCSC; uc003irh.3; human. [O43897-1]
DR CTD; 7092; -.
DR DisGeNET; 7092; -.
DR GeneCards; TLL1; -.
DR HGNC; HGNC:11843; TLL1.
DR HPA; ENSG00000038295; Group enriched (brain, placenta).
DR MalaCards; TLL1; -.
DR MIM; 606742; gene.
DR MIM; 613087; phenotype.
DR neXtProt; NX_O43897; -.
DR OpenTargets; ENSG00000038295; -.
DR Orphanet; 99106; Atrial septal defect, ostium primum type.
DR Orphanet; 99103; Atrial septal defect, ostium secundum type.
DR PharmGKB; PA36545; -.
DR VEuPathDB; HostDB:ENSG00000038295; -.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000157225; -.
DR HOGENOM; CLU_005140_0_0_1; -.
DR InParanoid; O43897; -.
DR PhylomeDB; O43897; -.
DR TreeFam; TF314351; -.
DR PathwayCommons; O43897; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-2214320; Anchoring fibril formation.
DR Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
DR SignaLink; O43897; -.
DR BioGRID-ORCS; 7092; 7 hits in 1069 CRISPR screens.
DR ChiTaRS; TLL1; human.
DR EvolutionaryTrace; O43897; -.
DR GeneWiki; TLL1; -.
DR GenomeRNAi; 7092; -.
DR Pharos; O43897; Tchem.
DR PRO; PR:O43897; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O43897; protein.
DR Bgee; ENSG00000038295; Expressed in secondary oocyte and 100 other tissues.
DR ExpressionAtlas; O43897; baseline and differential.
DR Genevisible; O43897; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030199; P:collagen fibril organization; TAS:Reactome.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR CDD; cd00041; CUB; 5.
DR CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR Gene3D; 2.60.120.290; -; 5.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR015446; BMP_1/tolloid-like.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR034036; ZnMP_TLD/BMP1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 5.
DR Pfam; PF07645; EGF_CA; 1.
DR PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 5.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49854; SSF49854; 5.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 5.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Atrial septal defect; Calcium;
KW Developmental protein; Differentiation; Disease variant; Disulfide bond;
KW EGF-like domain; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT PROPEP 31..147
FT /evidence="ECO:0000255"
FT /id="PRO_0000046023"
FT CHAIN 148..1013
FT /note="Tolloid-like protein 1"
FT /id="PRO_0000046024"
FT DOMAIN 148..347
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 349..461
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 462..574
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 574..615
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 618..730
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 730..770
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 774..886
FT /note="CUB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 887..1003
FT /note="CUB 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT ACT_SITE 241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 190..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211,
FT ECO:0000269|PubMed:18824173"
FT DISULFID 210..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 212..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 349..375
FT /evidence="ECO:0000250"
FT DISULFID 402..424
FT /evidence="ECO:0000250"
FT DISULFID 462..488
FT /evidence="ECO:0000250"
FT DISULFID 515..537
FT /evidence="ECO:0000250"
FT DISULFID 578..590
FT /evidence="ECO:0000250"
FT DISULFID 586..599
FT /evidence="ECO:0000250"
FT DISULFID 601..614
FT /evidence="ECO:0000250"
FT DISULFID 618..644
FT /evidence="ECO:0000250"
FT DISULFID 671..693
FT /evidence="ECO:0000250"
FT DISULFID 734..745
FT /evidence="ECO:0000250"
FT DISULFID 741..754
FT /evidence="ECO:0000250"
FT DISULFID 756..769
FT /evidence="ECO:0000250"
FT DISULFID 774..800
FT /evidence="ECO:0000250"
FT DISULFID 827..849
FT /evidence="ECO:0000250"
FT DISULFID 887..917
FT /evidence="ECO:0000250"
FT DISULFID 944..966
FT /evidence="ECO:0000250"
FT VAR_SEQ 387..392
FT /note="IVLNFT -> VVFSLC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017197"
FT VAR_SEQ 393..1013
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017198"
FT VARIANT 182
FT /note="M -> L (in ASD6; dbSNP:rs137852951)"
FT /evidence="ECO:0000269|PubMed:18830233"
FT /id="VAR_062519"
FT VARIANT 238
FT /note="V -> A (in ASD6; dbSNP:rs137852952)"
FT /evidence="ECO:0000269|PubMed:18830233"
FT /id="VAR_062520"
FT VARIANT 629
FT /note="I -> V (in ASD6; dbSNP:rs137852953)"
FT /evidence="ECO:0000269|PubMed:18830233"
FT /id="VAR_062521"
FT VARIANT 688
FT /note="L -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036142"
FT VARIANT 958
FT /note="T -> A (in dbSNP:rs2291822)"
FT /id="VAR_051585"
FT CONFLICT 156
FT /note="I -> V (in Ref. 2; AAF86287)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="N -> S (in Ref. 2; AAF86287)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="V -> A (in Ref. 2; AAF86287)"
FT /evidence="ECO:0000305"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:3EDI"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:3EDI"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:3EDI"
FT HELIX 172..188
FT /evidence="ECO:0007829|PDB:3EDI"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:3EDI"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:3EDI"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:3EDI"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:3EDI"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:3EDI"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3EDI"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3EDI"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:3EDI"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:3EDI"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:3EDI"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:3EDI"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:3EDI"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:3EDI"
FT HELIX 334..343
FT /evidence="ECO:0007829|PDB:3EDI"
SQ SEQUENCE 1013 AA; 114709 MW; 0FDDB6E8E9032DCC CRC64;
MGLGTLSPRM LVWLVASGIV FYGELWVCAG LDYDYTFDGN EEDKTETIDY KDPCKAAVFW
GDIALDDEDL NIFQIDRTID LTQNPFGNLG HTTGGLGDHA MSKKRGALYQ LIDRIRRIGF
GLEQNNTVKG KVPLQFSGQN EKNRVPRAAT SRTERIWPGG VIPYVIGGNF TGSQRAMFKQ
AMRHWEKHTC VTFIERSDEE SYIVFTYRPC GCCSYVGRRG NGPQAISIGK NCDKFGIVVH
ELGHVIGFWH EHTRPDRDNH VTIIRENIQP GQEYNFLKME PGEVNSLGER YDFDSIMHYA
RNTFSRGMFL DTILPSRDDN GIRPAIGQRT RLSKGDIAQA RKLYRCPACG ETLQESNGNL
SSPGFPNGYP SYTHCIWRVS VTPGEKIVLN FTTMDLYKSS LCWYDYIEVR DGYWRKSPLL
GRFCGDKLPE VLTSTDSRMW IEFRSSSNWV GKGFAAVYEA ICGGEIRKNE GQIQSPNYPD
DYRPMKECVW KITVSESYHV GLTFQSFEIE RHDNCAYDYL EVRDGTSENS PLIGRFCGYD
KPEDIRSTSN TLWMKFVSDG TVNKAGFAAN FFKEEDECAK PDRGGCEQRC LNTLGSYQCA
CEPGYELGPD RRSCEAACGG LLTKLNGTIT TPGWPKEYPP NKNCVWQVVA PTQYRISVKF
EFFELEGNEV CKYDYVEIWS GLSSESKLHG KFCGAEVPEV ITSQFNNMRI EFKSDNTVSK
KGFKAHFFSD KDECSKDNGG CQHECVNTMG SYMCQCRNGF VLHDNKHDCK EAECEQKIHS
PSGLITSPNW PDKYPSRKEC TWEISATPGH RIKLAFSEFE IEQHQECAYD HLEVFDGETE
KSPILGRLCG NKIPDPLVAT GNKMFVRFVS DASVQRKGFQ ATHSTECGGR LKAESKPRDL
YSHAQFGDNN YPGQVDCEWL LVSERGSRLE LSFQTFEVEE EADCGYDYVE LFDGLDSTAV
GLGRFCGSGP PEEIYSIGDS VLIHFHTDDT INKKGFHIRY KSIRYPDTTH TKK
