ID   HTRA3_HUMAN             Reviewed;         453 AA.
AC   P83110; Q7Z7A2;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 2.
DT   24-JUL-2024, entry version 186.
DE   RecName: Full=Serine protease HTRA3;
DE            EC=3.4.21.-;
DE   AltName: Full=High-temperature requirement factor A3;
DE   AltName: Full=Pregnancy-related serine protease;
DE   Flags: Precursor;
GN   Name=HTRA3; Synonyms=PRSP;
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC   TISSUE=Heart;
RX   PubMed=12513693; DOI=10.1042/bj20021569;
RA   Nie G.-Y., Hampton A., Li Y., Findlay J.K., Salamonsen L.A.;
RT   "Identification and cloning of two isoforms of human high-temperature
RT   requirement factor A3 (HtrA3), characterization of its genomic structure
RT   and comparison of its tissue distribution with HtrA1 and HtrA2.";
RL   Biochem. J. 371:39-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Southan C., Punia P.K.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Ovary;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16650464; DOI=10.1016/j.ygyno.2006.03.006;
RA   Bowden M.A., Di Nezza-Cossens L.A., Jobling T., Salamonsen L.A., Nie G.;
RT   "Serine proteases HTRA1 and HTRA3 are down-regulated with increasing grades
RT   of human endometrial cancer.";
RL   Gynecol. Oncol. 103:253-260(2006).
RN   [6]
RP   INDUCTION.
RX   PubMed=19424634; DOI=10.3892/or_00000385;
RA   Narkiewicz J., Lapinska-Szumczyk S., Zurawa-Janicka D., Skorko-Glonek J.,
RA   Emerich J., Lipinska B.;
RT   "Expression of human HtrA1, HtrA2, HtrA3 and TGF-beta1 genes in primary
RT   endometrial cancer.";
RL   Oncol. Rep. 21:1529-1537(2009).
RN   [7]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND POSSIBLE FUNCTION.
RX   PubMed=21321049; DOI=10.1093/humrep/der019;
RA   Singh H., Endo Y., Nie G.;
RT   "Decidual HtrA3 negatively regulates trophoblast invasion during human
RT   placentation.";
RL   Hum. Reprod. 26:748-757(2011).
RN   [8]
RP   INTERACTION WITH MYH9, MUTAGENESIS OF SER-305, ACTIVE SITE, AND FUNCTION.
RX   PubMed=22229724; DOI=10.2144/000113798;
RA   Singh H., Makino S., Endo Y., Li Y., Stephens A.N., Nie G.;
RT   "Application of the wheat-germ cell-free translation system to produce high
RT   temperature requirement A3 (HtrA3) proteases.";
RL   BioTechniques 52:23-28(2012).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 354-453 IN COMPLEX WITH SYNTHETIC
RP   PEPTIDES.
RX   PubMed=17962403; DOI=10.1110/ps.073049407;
RA   Runyon S.T., Zhang Y., Appleton B.A., Sazinsky S.L., Wu P., Pan B.,
RA   Wiesmann C., Skelton N.J., Sidhu S.S.;
RT   "Structural and functional analysis of the PDZ domains of human HtrA1 and
RT   HtrA3.";
RL   Protein Sci. 16:2454-2471(2007).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.27 ANGSTROMS) OF 130-453, SUBUNIT, AND ACTIVE
RP   SITE.
RX   PubMed=26110759; DOI=10.1371/journal.pone.0131142;
RA   Glaza P., Osipiuk J., Wenta T., Zurawa-Janicka D., Jarzab M., Lesner A.,
RA   Banecki B., Skorko-Glonek J., Joachimiak A., Lipinska B.;
RT   "Structural and functional analysis of human HtrA3 protease and its
RT   subdomains.";
RL   PLoS ONE 10:E0131142-E0131142(2015).
CC   -!- FUNCTION: Serine protease that cleaves beta-casein/CSN2 as well as
CC       several extracellular matrix (ECM) proteoglycans such as decorin/DCN,
CC       biglycan/BGN and fibronectin/FN1. Inhibits signaling mediated by TGF-
CC       beta family proteins possibly indirectly by degradation of these ECM
CC       proteoglycans (By similarity). May act as a tumor suppressor.
CC       Negatively regulates, in vitro, trophoblast invasion during placental
CC       development and may be involved in the development of the placenta in
CC       vivo. May also have a role in ovarian development, granulosa cell
CC       differentiation and luteinization (PubMed:21321049, PubMed:22229724).
CC       {ECO:0000250|UniProtKB:Q9D236, ECO:0000269|PubMed:21321049,
CC       ECO:0000269|PubMed:22229724}.
CC   -!- SUBUNIT: Homotrimer (PubMed:26110759). Interacts with TGFB1; the
CC       interaction inhibits TGFB-mediated signaling. Interacts with BMP4; the
CC       interaction inhibits BMP4-mediated signaling. Interacts with TGFB2 and
CC       GDF5 (By similarity). Interacts with MYH9.
CC       {ECO:0000250|UniProtKB:Q9D236, ECO:0000269|PubMed:17962403,
CC       ECO:0000269|PubMed:22229724, ECO:0000269|PubMed:26110759}.
CC   -!- INTERACTION:
CC       P83110; P60709: ACTB; NbExp=5; IntAct=EBI-2867394, EBI-353944;
CC       P83110; P83110: HTRA3; NbExp=3; IntAct=EBI-2867394, EBI-2867394;
CC       P83110; P83105: HTRA4; NbExp=5; IntAct=EBI-2867394, EBI-21776319;
CC       P83110; P17987: TCP1; NbExp=5; IntAct=EBI-2867394, EBI-356553;
CC       P83110; P98170: XIAP; NbExp=8; IntAct=EBI-2867394, EBI-517127;
CC       P83110; P02666: CSN2; Xeno; NbExp=8; IntAct=EBI-2867394, EBI-5260183;
CC       P83110-1; P83110-1: HTRA3; NbExp=2; IntAct=EBI-25469082, EBI-25469082;
CC       P83110-1; P17987: TCP1; NbExp=6; IntAct=EBI-25469082, EBI-356553;
CC       P83110-1; P08670: VIM; NbExp=4; IntAct=EBI-25469082, EBI-353844;
CC       P83110-1; P98170: XIAP; NbExp=7; IntAct=EBI-25469082, EBI-517127;
CC       P83110-2; P17987: TCP1; NbExp=7; IntAct=EBI-22017714, EBI-356553;
CC       P83110-2; P08670: VIM; NbExp=5; IntAct=EBI-22017714, EBI-353844;
CC       P83110-2; P98170: XIAP; NbExp=6; IntAct=EBI-22017714, EBI-517127;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21321049}.
CC       Note=Secretion increased during decidualization of endometrial stromal
CC       cells.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long, pL;
CC         IsoId=P83110-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short, pS;
CC         IsoId=P83110-2; Sequence=VSP_012570, VSP_012571;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in both adult
CC       and fetal heart, ovary, uterus placenta, and bladder. In the
CC       endometrium, expressed in epithelial glands and the stroma. Also
CC       present in leukocytes. Isoform 1 is predominant in heart and skeletal
CC       muscle, whereas isoform 2 is predominant in placenta and kidney.
CC       {ECO:0000269|PubMed:12513693, ECO:0000269|PubMed:16650464,
CC       ECO:0000269|PubMed:21321049}.
CC   -!- INDUCTION: Down-regulated in ovarian and endometrial cancers (EC).
CC       Decrease of 3.2-fold in endometrial cancer.
CC       {ECO:0000269|PubMed:16650464, ECO:0000269|PubMed:19424634}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/45757/HTRA3";
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DR   EMBL; AY280665; AAP42282.1; -; mRNA.
DR   EMBL; AY280666; AAP42283.1; -; mRNA.
DR   EMBL; AY040094; AAK71475.2; -; mRNA.
DR   EMBL; AC113611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC034390; AAH34390.1; -; mRNA.
DR   EMBL; BC035717; AAH35717.1; -; mRNA.
DR   CCDS; CCDS3400.1; -. [P83110-1]
DR   CCDS; CCDS75105.1; -. [P83110-2]
DR   RefSeq; NP_001284488.1; NM_001297559.1. [P83110-2]
DR   RefSeq; NP_444272.1; NM_053044.4. [P83110-1]
DR   PDB; 2P3W; X-ray; 1.70 A; A/B=354-453.
DR   PDB; 4RI0; X-ray; 3.27 A; A/B/C=130-453.
DR   PDBsum; 2P3W; -.
DR   PDBsum; 4RI0; -.
DR   AlphaFoldDB; P83110; -.
DR   SMR; P83110; -.
DR   BioGRID; 125099; 30.
DR   IntAct; P83110; 24.
DR   STRING; 9606.ENSP00000303766; -.
DR   BindingDB; P83110; -.
DR   MEROPS; S01.284; -.
DR   iPTMnet; P83110; -.
DR   PhosphoSitePlus; P83110; -.
DR   BioMuta; HTRA3; -.
DR   DMDM; 21542412; -.
DR   jPOST; P83110; -.
DR   MassIVE; P83110; -.
DR   PaxDb; 9606-ENSP00000303766; -.
DR   PeptideAtlas; P83110; -.
DR   ProteomicsDB; 57731; -. [P83110-1]
DR   ProteomicsDB; 57732; -. [P83110-2]
DR   Pumba; P83110; -.
DR   Antibodypedia; 9597; 126 antibodies from 26 providers.
DR   DNASU; 94031; -.
DR   Ensembl; ENST00000307358.7; ENSP00000303766.2; ENSG00000170801.10. [P83110-1]
DR   Ensembl; ENST00000382512.3; ENSP00000371952.3; ENSG00000170801.10. [P83110-2]
DR   GeneID; 94031; -.
DR   KEGG; hsa:94031; -.
DR   MANE-Select; ENST00000307358.7; ENSP00000303766.2; NM_053044.5; NP_444272.1.
DR   UCSC; uc003gkz.4; human. [P83110-1]
DR   AGR; HGNC:30406; -.
DR   CTD; 94031; -.
DR   DisGeNET; 94031; -.
DR   GeneCards; HTRA3; -.
DR   HGNC; HGNC:30406; HTRA3.
DR   HPA; ENSG00000170801; Tissue enhanced (heart).
DR   MIM; 608785; gene.
DR   neXtProt; NX_P83110; -.
DR   OpenTargets; ENSG00000170801; -.
DR   PharmGKB; PA134908281; -.
DR   VEuPathDB; HostDB:ENSG00000170801; -.
DR   eggNOG; ENOG502QT3F; Eukaryota.
DR   GeneTree; ENSGT00940000159570; -.
DR   HOGENOM; CLU_020120_6_2_1; -.
DR   InParanoid; P83110; -.
DR   OMA; AYVVTNH; -.
DR   OrthoDB; 2159919at2759; -.
DR   PhylomeDB; P83110; -.
DR   TreeFam; TF323480; -.
DR   BRENDA; 3.4.21.108; 2681.
DR   PathwayCommons; P83110; -.
DR   SignaLink; P83110; -.
DR   BioGRID-ORCS; 94031; 14 hits in 1148 CRISPR screens.
DR   EvolutionaryTrace; P83110; -.
DR   GenomeRNAi; 94031; -.
DR   Pharos; P83110; Tbio.
DR   PRO; PR:P83110; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; P83110; Protein.
DR   Bgee; ENSG00000170801; Expressed in apex of heart and 162 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR   CDD; cd00104; KAZAL_FS; 1.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.120; -; 1.
DR   Gene3D; 3.30.60.30; -; 1.
DR   Gene3D; 4.10.40.20; -; 1.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000867; IGFBP-like.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR   PANTHER; PTHR22939:SF14; SERINE PROTEASE HTRA3; 1.
DR   Pfam; PF00219; IGFBP; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00121; IB; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51323; IGFBP_N_2; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..453
FT                   /note="Serine protease HTRA3"
FT                   /id="PRO_0000026949"
FT   DOMAIN          21..84
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DOMAIN          64..128
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          359..444
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          175..340
FT                   /note="Serine protease"
FT   ACT_SITE        191
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:26110759"
FT   ACT_SITE        227
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:26110759"
FT   ACT_SITE        305
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:22229724,
FT                   ECO:0000269|PubMed:26110759"
FT   DISULFID        25..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        29..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        34..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        39..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        62..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        70..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        83..101
FT                   /evidence="ECO:0000305"
FT   DISULFID        90..126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   VAR_SEQ         351..357
FT                   /note="DWKKRFI -> APSLAVH (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12513693"
FT                   /id="VSP_012570"
FT   VAR_SEQ         358..453
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12513693"
FT                   /id="VSP_012571"
FT   MUTAGEN         305
FT                   /note="S->A: Abolishes protease activity. Stabilizes the
FT                   protein."
FT                   /evidence="ECO:0000269|PubMed:22229724"
FT   HELIX           136..139
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   HELIX           142..150
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   STRAND          154..161
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   STRAND          166..168
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   STRAND          171..181
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   TURN            182..184
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   STRAND          185..188
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   TURN            190..193
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   STRAND          203..208
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   STRAND          214..223
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   TURN            224..227
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   STRAND          228..233
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   STRAND          255..260
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   STRAND          268..274
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   STRAND          294..298
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   TURN            302..306
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   STRAND          307..310
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   STRAND          316..325
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   STRAND          328..333
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   HELIX           334..342
FT                   /evidence="ECO:0007829|PDB:4RI0"
FT   STRAND          354..356
FT                   /evidence="ECO:0007829|PDB:2P3W"
FT   STRAND          359..363
FT                   /evidence="ECO:0007829|PDB:2P3W"
FT   HELIX           366..375
FT                   /evidence="ECO:0007829|PDB:2P3W"
FT   STRAND          384..391
FT                   /evidence="ECO:0007829|PDB:2P3W"
FT   HELIX           396..400
FT                   /evidence="ECO:0007829|PDB:2P3W"
FT   STRAND          407..411
FT                   /evidence="ECO:0007829|PDB:2P3W"
FT   HELIX           419..428
FT                   /evidence="ECO:0007829|PDB:2P3W"
FT   STRAND          430..438
FT                   /evidence="ECO:0007829|PDB:2P3W"
FT   STRAND          441..447
FT                   /evidence="ECO:0007829|PDB:2P3W"
FT   STRAND          450..452
FT                   /evidence="ECO:0007829|PDB:2P3W"
SQ   SEQUENCE   453 AA;  48608 MW;  3046FCDA1AB24FA6 CRC64;
     MQARALLLAA LAALALAREP PAAPCPARCD VSRCPSPRCP GGYVPDLCNC CLVCAASEGE
     PCGGPLDSPC GESLECVRGL CRCRWSHAVC GTDGHTYANV CALQAASRRA LQLSGTPVRQ
     LQKGACPLGL HQLSSPRYKF NFIADVVEKI APAVVHIELF LRHPLFGRNV PLSSGSGFIM
     SEAGLIITNA HVVSSNSAAP GRQQLKVQLQ NGDSYEATIK DIDKKSDIAT IKIHPKKKLP
     VLLLGHSADL RPGEFVVAIG SPFALQNTVT TGIVSTAQRE GRELGLRDSD MDYIQTDAII
     NYGNSGGPLV NLDGEVIGIN TLKVTAGISF AIPSDRITRF LTEFQDKQIK DWKKRFIGIR
     MRTITPSLVD ELKASNPDFP EVSSGIYVQE VAPNSPSQRG GIQDGDIIVK VNGRPLVDSS
     ELQEAVLTES PLLLEVRRGN DDLLFSIAPE VVM
//