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   27-MAR-2024, entry version 169.
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; Evidence={ECO:0000255|PROSITE-
CC         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; 6.
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   GlyCosmos; O43897; 4 sites, 1 glycan.
DR   GlyGen; O43897; 7 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (2 sites).
DR   iPTMnet; O43897; -.
DR   PhosphoSitePlus; O43897; -.
DR   BioMuta; TLL1; -.
DR   MassIVE; O43897; -.
DR   MaxQB; O43897; -.
DR   PaxDb; 9606-ENSP00000061240; -.
DR   PeptideAtlas; O43897; -.
DR   ProteomicsDB; 49221; -. [O43897-1]
DR   ProteomicsDB; 49222; -. [O43897-2]
DR   Antibodypedia; 28327; 128 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   AGR; HGNC:11843; -.
DR   CTD; 7092; -.
DR   DisGeNET; 7092; -.
DR   GeneCards; TLL1; -.
DR   HGNC; HGNC:11843; TLL1.
DR   HPA; ENSG00000038295; Tissue enhanced (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   OrthoDB; 2873870at2759; -.
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 1149 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 101 other cell types or tissues.
DR   ExpressionAtlas; O43897; baseline and differential.
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; cd00054; EGF_CA; 1.
DR   CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 5.
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   PANTHER; PTHR24251:SF42; BONE MORPHOGENETIC PROTEIN 1; 1.
DR   PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00431; CUB; 5.
DR   Pfam; PF14670; FXa_inhibition; 2.
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; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 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.
DR   Genevisible; O43897; HS.
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
//