PCP_HUMAN
ID PCP_HUMAN Reviewed; 496 AA.
AC P42785; A8MU24; B2R7B7; B3KRK5; B5BU34;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Lysosomal Pro-X carboxypeptidase;
DE EC=3.4.16.2;
DE AltName: Full=Angiotensinase C;
DE AltName: Full=Lysosomal carboxypeptidase C;
DE AltName: Full=Proline carboxypeptidase;
DE AltName: Full=Prolylcarboxypeptidase;
DE Short=PRCP;
DE Flags: Precursor;
GN Name=PRCP; Synonyms=PCP;
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), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Kidney;
RX PubMed=8344943; DOI=10.1016/s0021-9258(19)85465-0;
RA Tan F., Morris P.W., Skidgel R.A., Erdoes E.G.;
RT "Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C).
RT Similarity to both serine carboxypeptidase and prolylendopeptidase
RT families.";
RL J. Biol. Chem. 268:16631-16638(1993).
RN [2]
RP ERRATUM OF PUBMED:8344943.
RA Tan F., Morris P.W., Skidgel R.A., Erdoes E.G.;
RL J. Biol. Chem. 268:26032-26032(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ASP-112.
RC TISSUE=Kidney, and Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [8]
RP CHARACTERIZATION.
RC TISSUE=Kidney;
RX PubMed=28321; DOI=10.1016/s0021-9258(17)34557-x;
RA Odya C.E., Marinkovic D.V., Hammon K.J., Stewart T.A., Erdos E.G.;
RT "Purification and properties of prolylcarboxypeptidase (angiotensinase C)
RT from human kidney.";
RL J. Biol. Chem. 253:5927-5931(1978).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-317 AND ASN-415.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 46-491, SUBUNIT, DISULFIDE BONDS,
RP ACTIVE SITE, AND GLYCOSYLATION AT ASN-101; ASN-317; ASN-336; ASN-345 AND
RP ASN-415.
RX PubMed=20540760; DOI=10.1186/1472-6807-10-16;
RA Soisson S.M., Patel S.B., Abeywickrema P.D., Byrne N.J., Diehl R.E.,
RA Hall D.L., Ford R.E., Reid J.C., Rickert K.W., Shipman J.M., Sharma S.,
RA Lumb K.J.;
RT "Structural definition and substrate specificity of the S28 protease
RT family: the crystal structure of human prolylcarboxypeptidase.";
RL BMC Struct. Biol. 10:16-16(2010).
CC -!- FUNCTION: Cleaves C-terminal amino acids linked to proline in peptides
CC such as angiotensin II, III and des-Arg9-bradykinin. This cleavage
CC occurs at acidic pH, but enzymatic activity is retained with some
CC substrates at neutral pH.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of a -Pro-|-Xaa bond to release a C-terminal amino
CC acid.; EC=3.4.16.2;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20540760}.
CC -!- INTERACTION:
CC P42785; O60883: GPR37L1; NbExp=2; IntAct=EBI-2803892, EBI-2927498;
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P42785-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P42785-2; Sequence=VSP_045799;
CC -!- TISSUE SPECIFICITY: Highest levels in placenta, lung and liver. Also
CC present in heart, brain, pancreas and kidney.
CC -!- SIMILARITY: Belongs to the peptidase S28 family. {ECO:0000305}.
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DR EMBL; L13977; AAA99891.1; -; mRNA.
DR EMBL; AK091786; BAG52417.1; -; mRNA.
DR EMBL; AK312919; BAG35764.1; -; mRNA.
DR EMBL; AB451270; BAG70084.1; -; mRNA.
DR EMBL; AB451397; BAG70211.1; -; mRNA.
DR EMBL; AP000893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW75074.1; -; Genomic_DNA.
DR EMBL; CH471076; EAW75075.1; -; Genomic_DNA.
DR EMBL; BC001500; AAH01500.1; -; mRNA.
DR CCDS; CCDS41695.1; -. [P42785-2]
DR CCDS; CCDS8262.1; -. [P42785-1]
DR PIR; A47352; A47352.
DR RefSeq; NP_001306143.1; NM_001319214.1.
DR RefSeq; NP_005031.1; NM_005040.3. [P42785-1]
DR RefSeq; NP_955450.2; NM_199418.3. [P42785-2]
DR PDB; 3N2Z; X-ray; 2.79 A; B=46-491.
DR PDBsum; 3N2Z; -.
DR AlphaFoldDB; P42785; -.
DR SMR; P42785; -.
DR BioGRID; 111538; 44.
DR IntAct; P42785; 10.
DR STRING; 9606.ENSP00000377055; -.
DR BindingDB; P42785; -.
DR ChEMBL; CHEMBL2335; -.
DR DrugCentral; P42785; -.
DR GuidetoPHARMACOLOGY; 1584; -.
DR ESTHER; human-PRCP; Prolylcarboxypeptidase.
DR MEROPS; S28.001; -.
DR GlyConnect; 1478; 9 N-Linked glycans (2 sites).
DR GlyGen; P42785; 8 sites, 9 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P42785; -.
DR MetOSite; P42785; -.
DR PhosphoSitePlus; P42785; -.
DR BioMuta; PRCP; -.
DR DMDM; 1172047; -.
DR EPD; P42785; -.
DR jPOST; P42785; -.
DR MassIVE; P42785; -.
DR MaxQB; P42785; -.
DR PaxDb; P42785; -.
DR PeptideAtlas; P42785; -.
DR PRIDE; P42785; -.
DR ProteomicsDB; 2074; -.
DR ProteomicsDB; 55558; -. [P42785-1]
DR Antibodypedia; 2472; 260 antibodies from 27 providers.
DR DNASU; 5547; -.
DR Ensembl; ENST00000313010.8; ENSP00000317362.3; ENSG00000137509.12. [P42785-1]
DR Ensembl; ENST00000393399.6; ENSP00000377055.2; ENSG00000137509.12. [P42785-2]
DR GeneID; 5547; -.
DR KEGG; hsa:5547; -.
DR MANE-Select; ENST00000313010.8; ENSP00000317362.3; NM_005040.4; NP_005031.1.
DR UCSC; uc001ozr.4; human. [P42785-1]
DR CTD; 5547; -.
DR DisGeNET; 5547; -.
DR GeneCards; PRCP; -.
DR HGNC; HGNC:9344; PRCP.
DR HPA; ENSG00000137509; Low tissue specificity.
DR MIM; 176785; gene.
DR neXtProt; NX_P42785; -.
DR OpenTargets; ENSG00000137509; -.
DR PharmGKB; PA33705; -.
DR VEuPathDB; HostDB:ENSG00000137509; -.
DR eggNOG; KOG2183; Eukaryota.
DR GeneTree; ENSGT00940000158099; -.
DR HOGENOM; CLU_020959_0_0_1; -.
DR InParanoid; P42785; -.
DR OMA; TLEDYAM; -.
DR OrthoDB; 555765at2759; -.
DR PhylomeDB; P42785; -.
DR TreeFam; TF314414; -.
DR BRENDA; 3.4.16.2; 2681.
DR PathwayCommons; P42785; -.
DR Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P42785; -.
DR SIGNOR; P42785; -.
DR BioGRID-ORCS; 5547; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; PRCP; human.
DR EvolutionaryTrace; P42785; -.
DR GeneWiki; PRCP; -.
DR GenomeRNAi; 5547; -.
DR Pharos; P42785; Tchem.
DR PRO; PR:P42785; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P42785; protein.
DR Bgee; ENSG00000137509; Expressed in tendon of biceps brachii and 211 other tissues.
DR ExpressionAtlas; P42785; baseline and differential.
DR Genevisible; P42785; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0045178; C:basal part of cell; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; TAS:ProtInc.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; IBA:GO_Central.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0002353; P:plasma kallikrein-kinin cascade; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; IBA:GO_Central.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; IEA:Ensembl.
DR Gene3D; 1.20.120.980; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR008758; Peptidase_S28.
DR InterPro; IPR042269; Ser_carbopepase_S28_SKS.
DR Pfam; PF05577; Peptidase_S28; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Carboxypeptidase;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Protease; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..45
FT /id="PRO_0000027308"
FT CHAIN 46..496
FT /note="Lysosomal Pro-X carboxypeptidase"
FT /id="PRO_0000027309"
FT REGION 194..334
FT /note="SKS domain"
FT ACT_SITE 179
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:20540760"
FT ACT_SITE 430
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:20540760"
FT ACT_SITE 455
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:20540760"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20540760"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:20540760"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20540760"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20540760"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:20540760"
FT DISULFID 215..372
FT /evidence="ECO:0000269|PubMed:20540760"
FT DISULFID 233..310
FT /evidence="ECO:0000269|PubMed:20540760"
FT DISULFID 264..343
FT /evidence="ECO:0000269|PubMed:20540760"
FT DISULFID 364..394
FT /evidence="ECO:0000269|PubMed:20540760"
FT VAR_SEQ 56
FT /note="K -> KALAAGQLHICIIQLNHYKTPL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045799"
FT VARIANT 112
FT /note="E -> D (in dbSNP:rs2229437)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_020464"
FT VARIANT 444
FT /note="T -> S (in dbSNP:rs2228312)"
FT /id="VAR_029329"
FT CONFLICT 104
FT /note="G -> E (in Ref. 3; BAG52417)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="S -> L (in Ref. 3; BAG52417)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="W -> R (in Ref. 3; BAG52417)"
FT /evidence="ECO:0000305"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:3N2Z"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:3N2Z"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:3N2Z"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:3N2Z"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:3N2Z"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:3N2Z"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:3N2Z"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:3N2Z"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 233..247
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:3N2Z"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 272..288
FT /evidence="ECO:0007829|PDB:3N2Z"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 305..312
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 320..336
FT /evidence="ECO:0007829|PDB:3N2Z"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 354..365
FT /evidence="ECO:0007829|PDB:3N2Z"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 387..398
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 406..411
FT /evidence="ECO:0007829|PDB:3N2Z"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 431..435
FT /evidence="ECO:0007829|PDB:3N2Z"
FT STRAND 441..450
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:3N2Z"
FT HELIX 468..489
FT /evidence="ECO:0007829|PDB:3N2Z"
SQ SEQUENCE 496 AA; 55800 MW; FC5DD570D3D3AB4F CRC64;
MGRRALLLLL LSFLAPWATI ALRPALRALG SLHLPTNPTS LPAVAKNYSV LYFQQKVDHF
GFNTVKTFNQ RYLVADKYWK KNGGSILFYT GNEGDIIWFC NNTGFMWDVA EELKAMLVFA
EHRYYGESLP FGDNSFKDSR HLNFLTSEQA LADFAELIKH LKRTIPGAEN QPVIAIGGSY
GGMLAAWFRM KYPHMVVGAL AASAPIWQFE DLVPCGVFMK IVTTDFRKSG PHCSESIHRS
WDAINRLSNT GSGLQWLTGA LHLCSPLTSQ DIQHLKDWIS ETWVNLAMVD YPYASNFLQP
LPAWPIKVVC QYLKNPNVSD SLLLQNIFQA LNVYYNYSGQ VKCLNISETA TSSLGTLGWS
YQACTEVVMP FCTNGVDDMF EPHSWNLKEL SDDCFQQWGV RPRPSWITTM YGGKNISSHT
NIVFSNGELD PWSGGGVTKD ITDTLVAVTI SEGAHHLDLR TKNALDPMSV LLARSLEVRH
MKNWIRDFYD SAGKQH
