ID   TIMP2_HUMAN             Reviewed;         220 AA.
AC   P16035; Q16121; Q93006; Q9UDF7;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   27-MAR-2024, entry version 221.
DE   RecName: Full=Metalloproteinase inhibitor 2;
DE   AltName: Full=CSC-21K;
DE   AltName: Full=Tissue inhibitor of metalloproteinases 2;
DE            Short=TIMP-2;
DE   Flags: Precursor;
GN   Name=TIMP2;
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], AND INDUCTION.
RX   PubMed=2380196; DOI=10.1016/s0021-9258(18)77438-3;
RA   Stetler-Stevenson W.G., Brown P.D., Onisto M., Levy A.T., Liotta L.A.;
RT   "Tissue inhibitor of metalloproteinases-2 (TIMP-2) mRNA expression in tumor
RT   cell lines and human tumor tissues.";
RL   J. Biol. Chem. 265:13933-13938(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2157214; DOI=10.1073/pnas.87.7.2800;
RA   Boone T.C., Johnson M.J., de Clerck Y.A., Langley K.E.;
RT   "cDNA cloning and expression of a metalloproteinase inhibitor related to
RT   tissue inhibitor of metalloproteinases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:2800-2804(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   PubMed=8810321; DOI=10.1074/jbc.271.41.25498;
RA   Hammani K., Blakis A., Morsette D., Bowcock A., Schmutte C., Henriet P.,
RA   Declerck Y.A.;
RT   "Structure and characterization of the human tissue inhibitor of
RT   metalloproteinases-2 gene.";
RL   J. Biol. Chem. 271:25498-25505(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta, and Skin;
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   NUCLEOTIDE SEQUENCE OF 30-214.
RA   Malik K., Sejima H., Aoki T., Iwata K.;
RL   Submitted (AUG-1990) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PROTEIN SEQUENCE OF 27-219, AND FUNCTION.
RX   PubMed=2793861; DOI=10.1016/s0021-9258(18)71503-2;
RA   Stetler-Stevenson W.G., Krutzsch H.C., Liotta L.A.;
RT   "Tissue inhibitor of metalloproteinase (TIMP-2). A new member of the
RT   metalloproteinase inhibitor family.";
RL   J. Biol. Chem. 264:17374-17378(1989).
RN   [7]
RP   PROTEIN SEQUENCE OF 27-219.
RX   PubMed=1480041;
RA   Stetler-Stevenson W.G., Krutzsch H.C., Liotta L.A.;
RT   "TIMP-2: identification and characterization of a new member of the
RT   metalloproteinase inhibitor family.";
RL   Matrix Suppl. 1:299-306(1992).
RN   [8]
RP   PROTEIN SEQUENCE OF 30-51; 124-141 AND 159-173, AND FUNCTION.
RX   PubMed=2554304; DOI=10.1073/pnas.86.21.8207;
RA   Goldberg G.I., Marmer B.L., Grant G.A., Eisen A.Z., Wilhelm S., He C.;
RT   "Human 72-kilodalton type IV collagenase forms a complex with a tissue
RT   inhibitor of metalloproteases designated TIMP-2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:8207-8211(1989).
RN   [9]
RP   PROTEIN SEQUENCE OF 27-41.
RC   TISSUE=Synovial fluid;
RX   PubMed=1730286; DOI=10.1016/0014-5793(92)80393-u;
RA   Osthues A., Knaueper V., Oberhoff R., Reinke H., Tschesche H.;
RT   "Isolation and characterization of tissue inhibitors of metalloproteinases
RT   (TIMP-1 and TIMP-2) from human rheumatoid synovial fluid.";
RL   FEBS Lett. 296:16-20(1992).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RX   PubMed=8112602; DOI=10.1016/0378-1119(94)90753-6;
RA   de Clerck Y.A., Darville M.I., Eeckhout Y., Rousseau G.G.;
RT   "Characterization of the promoter of the gene encoding human tissue
RT   inhibitor of metalloproteinases-2 (TIMP-2).";
RL   Gene 139:185-191(1994).
RN   [11]
RP   INTERACTION WITH MMP2.
RX   PubMed=1655733; DOI=10.1016/s0021-9258(18)55224-8;
RA   Howard E.W., Banda M.J.;
RT   "Binding of tissue inhibitor of metalloproteinases 2 to two distinct sites
RT   on human 72-kDa gelatinase. Identification of a stabilization site.";
RL   J. Biol. Chem. 266:17972-17977(1991).
RN   [12]
RP   INTERACTION WITH MMP2, AND FUNCTION.
RX   PubMed=11710594; DOI=10.1007/s004320100271;
RA   Chattopadhyay N., Mitra A., Frei E., Chatterjee A.;
RT   "Human cervical tumor cell (SiHa) surface alphavbeta3 integrin receptor has
RT   associated matrix metalloproteinase (MMP-2) activity.";
RL   J. Cancer Res. Clin. Oncol. 127:653-658(2001).
RN   [13]
RP   STRUCTURE BY NMR OF 27-153.
RX   PubMed=7918391; DOI=10.1021/bi00205a010;
RA   Williamson R.A., Martorell G., Carr M.D., Murphy G., Docherty A.J.P.,
RA   Freedman R.B., Feeney J.;
RT   "Solution structure of the active domain of tissue inhibitor of
RT   metalloproteinases-2. A new member of the OB fold protein family.";
RL   Biochemistry 33:11745-11759(1994).
RN   [14]
RP   STRUCTURE BY NMR OF 27-153.
RX   PubMed=9705310; DOI=10.1074/jbc.273.34.21736;
RA   Muskett F.W., Frenkiel T.A., Feeney J., Freedman R.B., Carr M.D.,
RA   Williamson R.A.;
RT   "High resolution structure of the N-terminal domain of tissue inhibitor of
RT   metalloproteinases-2 and characterization of its interaction site with
RT   matrix metalloproteinase-3.";
RL   J. Biol. Chem. 273:21736-21743(1998).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-220.
RX   PubMed=9837731; DOI=10.1006/jmbi.1998.2223;
RA   Tuuttila A., Morgunova E., Bergmann U., Lindqvist Y., Maskos K.,
RA   Fernandez-Catalan C., Bode W., Tryggvason K., Schneider G.;
RT   "Three-dimensional structure of human tissue inhibitor of
RT   metalloproteinases-2 at 2.1-A resolution.";
RL   J. Mol. Biol. 284:1133-1140(1998).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH MMP-2, AND DISULFIDE
RP   BOND.
RX   PubMed=12032297; DOI=10.1073/pnas.102185399;
RA   Morgunova E., Tuuttila A., Bergmann U., Tryggvason K.;
RT   "Structural insight into the complex formation of latent matrix
RT   metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:7414-7419(2002).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-220 IN COMPLEX WITH MMP10 AND
RP   ZINC.
RX   PubMed=24073280; DOI=10.1371/journal.pone.0075836;
RA   Batra J., Soares A.S., Mehner C., Radisky E.S.;
RT   "Matrix metalloproteinase-10/TIMP-2 structure and analyses define conserved
RT   core interactions and diverse exosite interactions in MMP/TIMP complexes.";
RL   PLoS ONE 8:E75836-E75836(2013).
CC   -!- FUNCTION: Complexes with metalloproteinases (such as collagenases) and
CC       irreversibly inactivates them by binding to their catalytic zinc
CC       cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9,
CC       MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.
CC       {ECO:0000269|PubMed:11710594, ECO:0000269|PubMed:2554304,
CC       ECO:0000269|PubMed:2793861}.
CC   -!- SUBUNIT: Interacts (via the C-terminal) with MMP2 (via the C-terminal
CC       PEX domain); the interaction inhibits the MMP2 activity.
CC       {ECO:0000269|PubMed:11710594, ECO:0000269|PubMed:12032297,
CC       ECO:0000269|PubMed:1655733}.
CC   -!- INTERACTION:
CC       P16035; P50281: MMP14; NbExp=2; IntAct=EBI-1033507, EBI-992788;
CC       P16035; P08253: MMP2; NbExp=2; IntAct=EBI-1033507, EBI-1033518;
CC       P16035; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-1033507, EBI-947187;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: Down-regulated by TGFB1. {ECO:0000269|PubMed:2380196}.
CC   -!- PTM: The activity of TIMP2 is dependent on the presence of disulfide
CC       bonds.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/42572/TIMP2";
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DR   EMBL; J05593; AAA61186.1; -; mRNA.
DR   EMBL; S48568; AAB19474.1; -; mRNA.
DR   EMBL; U44385; AAC50729.1; -; Genomic_DNA.
DR   EMBL; U44381; AAC50729.1; JOINED; Genomic_DNA.
DR   EMBL; U44382; AAC50729.1; JOINED; Genomic_DNA.
DR   EMBL; U44383; AAC50729.1; JOINED; Genomic_DNA.
DR   EMBL; M32304; AAA59581.1; -; mRNA.
DR   EMBL; BC052605; AAH52605.1; -; mRNA.
DR   EMBL; BC071586; AAH71586.1; -; mRNA.
DR   EMBL; X54533; CAA38400.1; -; mRNA.
DR   EMBL; S68860; AAD14025.1; -; Genomic_DNA.
DR   CCDS; CCDS11758.1; -.
DR   PIR; A37128; A37128.
DR   PIR; I53729; I53729.
DR   RefSeq; NP_003246.1; NM_003255.4.
DR   PDB; 1BR9; X-ray; 2.10 A; A=27-220.
DR   PDB; 1GXD; X-ray; 3.10 A; C/D=27-220.
DR   PDB; 2TMP; NMR; -; A=27-153.
DR   PDB; 4ILW; X-ray; 2.10 A; A/B=27-220.
DR   PDBsum; 1BR9; -.
DR   PDBsum; 1GXD; -.
DR   PDBsum; 2TMP; -.
DR   PDBsum; 4ILW; -.
DR   AlphaFoldDB; P16035; -.
DR   BMRB; P16035; -.
DR   SMR; P16035; -.
DR   BioGRID; 112933; 41.
DR   IntAct; P16035; 7.
DR   MINT; P16035; -.
DR   STRING; 9606.ENSP00000262768; -.
DR   MEROPS; I35.002; -.
DR   iPTMnet; P16035; -.
DR   PhosphoSitePlus; P16035; -.
DR   SwissPalm; P16035; -.
DR   BioMuta; TIMP2; -.
DR   DMDM; 135854; -.
DR   DOSAC-COBS-2DPAGE; P16035; -.
DR   EPD; P16035; -.
DR   jPOST; P16035; -.
DR   MassIVE; P16035; -.
DR   MaxQB; P16035; -.
DR   PaxDb; 9606-ENSP00000262768; -.
DR   PeptideAtlas; P16035; -.
DR   ProteomicsDB; 53263; -.
DR   Pumba; P16035; -.
DR   TopDownProteomics; P16035; -.
DR   Antibodypedia; 4126; 1395 antibodies from 44 providers.
DR   DNASU; 7077; -.
DR   Ensembl; ENST00000262768.11; ENSP00000262768.6; ENSG00000035862.13.
DR   GeneID; 7077; -.
DR   KEGG; hsa:7077; -.
DR   MANE-Select; ENST00000262768.11; ENSP00000262768.6; NM_003255.5; NP_003246.1.
DR   UCSC; uc002jwf.4; human.
DR   AGR; HGNC:11821; -.
DR   CTD; 7077; -.
DR   DisGeNET; 7077; -.
DR   GeneCards; TIMP2; -.
DR   HGNC; HGNC:11821; TIMP2.
DR   HPA; ENSG00000035862; Tissue enhanced (ovary).
DR   MIM; 188825; gene.
DR   neXtProt; NX_P16035; -.
DR   OpenTargets; ENSG00000035862; -.
DR   PharmGKB; PA36527; -.
DR   VEuPathDB; HostDB:ENSG00000035862; -.
DR   eggNOG; KOG4745; Eukaryota.
DR   GeneTree; ENSGT00940000158348; -.
DR   InParanoid; P16035; -.
DR   OMA; SAQDECL; -.
DR   OrthoDB; 5403389at2759; -.
DR   PhylomeDB; P16035; -.
DR   TreeFam; TF317409; -.
DR   BRENDA; 3.4.24.22; 2681.
DR   PathwayCommons; P16035; -.
DR   Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; P16035; -.
DR   SIGNOR; P16035; -.
DR   BioGRID-ORCS; 7077; 20 hits in 1153 CRISPR screens.
DR   ChiTaRS; TIMP2; human.
DR   EvolutionaryTrace; P16035; -.
DR   GeneWiki; TIMP2; -.
DR   GenomeRNAi; 7077; -.
DR   Pharos; P16035; Tbio.
DR   PRO; PR:P16035; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P16035; Protein.
DR   Bgee; ENSG00000035862; Expressed in tendon of biceps brachii and 199 other cell types or tissues.
DR   ExpressionAtlas; P16035; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR   GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR   GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0140678; F:molecular function inhibitor activity; IMP:DisProt.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IBA:GO_Central.
DR   GO; GO:1905049; P:negative regulation of metallopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR   GO; GO:0009725; P:response to hormone; IBA:GO_Central.
DR   CDD; cd03585; NTR_TIMP; 1.
DR   Gene3D; 2.40.50.120; -; 1.
DR   Gene3D; 3.90.370.10; Tissue inhibitor of metalloproteinase-1. Chain B, domain 1; 1.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR001820; TIMP.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   InterPro; IPR027465; TIMP_C.
DR   InterPro; IPR030490; TIMP_CS.
DR   PANTHER; PTHR11844; METALLOPROTEASE INHIBITOR; 1.
DR   PANTHER; PTHR11844:SF24; METALLOPROTEINASE INHIBITOR 2; 1.
DR   Pfam; PF00965; TIMP; 1.
DR   SMART; SM00206; NTR; 1.
DR   SUPFAM; SSF50242; TIMP-like; 1.
DR   PROSITE; PS50189; NTR; 1.
DR   PROSITE; PS00288; TIMP; 1.
DR   Genevisible; P16035; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Metal-binding;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:1480041,
FT                   ECO:0000269|PubMed:1730286, ECO:0000269|PubMed:2793861"
FT   CHAIN           27..220
FT                   /note="Metalloproteinase inhibitor 2"
FT                   /id="PRO_0000034335"
FT   DOMAIN          27..152
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   REGION          27..30
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000269|PubMed:24073280,
FT                   ECO:0007744|PDB:4ILW"
FT   REGION          95..96
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000269|PubMed:24073280,
FT                   ECO:0007744|PDB:4ILW"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared with metalloproteinase partner"
FT                   /evidence="ECO:0000269|PubMed:24073280,
FT                   ECO:0007744|PDB:4ILW"
FT   SITE            40
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000269|PubMed:24073280,
FT                   ECO:0007744|PDB:4ILW"
FT   SITE            61
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000269|PubMed:24073280,
FT                   ECO:0007744|PDB:4ILW"
FT   SITE            67
FT                   /note="Involved in metalloproteinase-binding"
FT                   /evidence="ECO:0000269|PubMed:24073280,
FT                   ECO:0007744|PDB:4ILW"
FT   DISULFID        27..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295,
FT                   ECO:0000269|PubMed:12032297"
FT   DISULFID        29..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295,
FT                   ECO:0000269|PubMed:12032297"
FT   DISULFID        39..152
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295,
FT                   ECO:0000269|PubMed:12032297"
FT   DISULFID        154..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295,
FT                   ECO:0000269|PubMed:12032297"
FT   DISULFID        159..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295,
FT                   ECO:0000269|PubMed:12032297"
FT   DISULFID        172..193
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295,
FT                   ECO:0000269|PubMed:12032297"
FT   CONFLICT        17..19
FT                   /note="LAT -> P (in Ref. 3; AAC50729)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44..50
FT                   /note="VIRAKAV -> GKESGDP (in Ref. 10)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        78
FT                   /note="M -> K (in Ref. 6; AA sequence and 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82
FT                   /note="P -> I (in Ref. 6; AA sequence and 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        96
FT                   /note="A -> V (in Ref. 5; CAA38400)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="S -> E (in Ref. 6; AA sequence and 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        118
FT                   /note="Missing (in Ref. 6; AA sequence and 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="M -> R (in Ref. 6; AA sequence and 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        150
FT                   /note="M -> Q (in Ref. 6; AA sequence and 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        175
FT                   /note="M -> T (in Ref. 6; AA sequence and 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           34..40
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   STRAND          41..59
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:4ILW"
FT   STRAND          65..81
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   STRAND          88..91
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   TURN            104..107
FT                   /evidence="ECO:0007829|PDB:4ILW"
FT   STRAND          109..118
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   HELIX           138..143
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   TURN            144..148
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   STRAND          154..158
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   STRAND          171..174
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   HELIX           176..180
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   STRAND          181..185
FT                   /evidence="ECO:0007829|PDB:1GXD"
FT   HELIX           186..190
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   STRAND          192..195
FT                   /evidence="ECO:0007829|PDB:1BR9"
FT   STRAND          197..199
FT                   /evidence="ECO:0007829|PDB:4ILW"
FT   STRAND          201..204
FT                   /evidence="ECO:0007829|PDB:1BR9"
SQ   SEQUENCE   220 AA;  24399 MW;  603E5B1C9F94735D CRC64;
     MGAAARTLRL ALGLLLLATL LRPADACSCS PVHPQQAFCN ADVVIRAKAV SEKEVDSGND
     IYGNPIKRIQ YEIKQIKMFK GPEKDIEFIY TAPSSAVCGV SLDVGGKKEY LIAGKAEGDG
     KMHITLCDFI VPWDTLSTTQ KKSLNHRYQM GCECKITRCP MIPCYISSPD ECLWMDWVTE
     KNINGHQAKF FACIKRSDGS CAWYRGAAPP KQEFLDIEDP
//