ID PTX3_HUMAN Reviewed; 381 AA. AC P26022; B2R6T6; Q38M82; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 24-JAN-2024, entry version 189. DE RecName: Full=Pentraxin-related protein PTX3 {ECO:0000305}; DE AltName: Full=Pentaxin-related protein PTX3; DE AltName: Full=Tumor necrosis factor alpha-induced protein 5; DE Short=TNF alpha-induced protein 5; DE AltName: Full=Tumor necrosis factor-inducible gene 14 protein; DE Short=TSG-14; DE Flags: Precursor; GN Name=PTX3 {ECO:0000312|HGNC:HGNC:9692}; Synonyms=TNFAIP5, TSG14; 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 VARIANT ASP-48. RC TISSUE=Endothelial cell; RX PubMed=1429570; DOI=10.1016/s0021-9258(18)41653-5; RA Breviario F., D'Aniello E.M., Golay J., Peri G., Bottazi B., Bairoch A., RA Saccone S., Marzella R., Predazzi V., Rocchi M., Della Valle G., Dejana E., RA Mantovani A., Introna M.; RT "Interleukin-1-inducible genes in endothelial cells. Cloning of a new gene RT related to C-reactive protein and serum amyloid P component."; RL J. Biol. Chem. 267:22190-22197(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-48. RC TISSUE=Endothelial cell; RX PubMed=8131794; RA Introna M., Breviario F., D'Aniello E.M., Golay J., Dejana E., RA Mantovani A.; RT "IL-1 inducible genes in human umbilical vein endothelial cells."; RL Eur. Heart J. 14:78-81(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-48. RC TISSUE=Foreskin; RX PubMed=7679696; RA Lee G.W., Lee T.H., Vilcek J.; RT "TSG-14, a tumor necrosis factor- and IL-1-inducible protein, is a novel RT member of the pentaxin family of acute phase proteins."; RL J. Immunol. 150:1804-1812(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Tan J., Davila S., Hibberd M.L., Seielstad M.; RT "Genetic variation in pentaxin-related protein PTX3."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [7] 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-48. 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 [9] RP DISCUSSION OF SEQUENCE. RX PubMed=7523502; RA Lee G.W., Goodman A.R., Lee T.H., Vilcek J.; RT "Relationship of TSG-14 protein to the pentraxin family of major acute RT phase proteins."; RL J. Immunol. 153:3700-3707(1994). RN [10] RP REVIEW. RX PubMed=12763682; DOI=10.1016/s0264-410x(03)00199-3; RA Mantovani A., Garlanda C., Bottazzi B.; RT "Pentraxin 3, a non-redundant soluble pattern recognition receptor involved RT in innate immunity."; RL Vaccine 21:S43-S47(2003). RN [11] RP SUBUNIT, AND DISULFIDE BONDS. RX PubMed=18223257; DOI=10.1074/jbc.m708535200; RA Inforzato A., Rivieccio V., Morreale A.P., Bastone A., Salustri A., RA Scarchilli L., Verdoliva A., Vincenti S., Gallo G., Chiapparino C., RA Pacello L., Nucera E., Serlupi-Crescenzi O., Day A.J., Bottazzi B., RA Mantovani A., De Santis R., Salvatori G.; RT "Structural characterization of PTX3 disulfide bond network and its RT multimeric status in cumulus matrix organization."; RL J. Biol. Chem. 283:10147-10161(2008). RN [12] RP INTERACTION WITH SARS-COV-2 NUCLEOPROTEIN AND SPIKE GLYCOPROTEIN (MICROBIAL RP FUNCTION). RX PubMed=35102342; DOI=10.1038/s41590-021-01114-w; RA Stravalaci M., Pagani I., Paraboschi E.M., Pedotti M., Doni A., RA Scavello F., Mapelli S.N., Sironi M., Perucchini C., Varani L., RA Matkovic M., Cavalli A., Cesana D., Gallina P., Pedemonte N., Capurro V., RA Clementi N., Mancini N., Invernizzi P., Bayarri-Olmos R., Garred P., RA Rappuoli R., Duga S., Bottazzi B., Uguccioni M., Asselta R., Vicenzi E., RA Mantovani A., Garlanda C.; RT "Recognition and inhibition of SARS-CoV-2 by humoral innate immunity RT pattern recognition molecules."; RL Nat. Immunol. 23:275-286(2022). CC -!- FUNCTION: Plays a role in the regulation of innate resistance to CC pathogens, inflammatory reactions, possibly clearance of self- CC components and female fertility. {ECO:0000305|PubMed:12763682}. CC -!- SUBUNIT: Homooctamer; disulfide-linked (PubMed:18223257). Binds to C1q CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:18223257}. CC -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus-2/SARS- CC CoV-2 Nucleoprotein and Spike protein homotrimer. CC {ECO:0000269|PubMed:35102342}. CC -!- INTERACTION: CC P26022; P08603: CFH; NbExp=15; IntAct=EBI-11574553, EBI-1223708; CC P26022; P08603-2: CFH; NbExp=2; IntAct=EBI-11574553, EBI-12684810; CC P26022; O00602: FCN1; NbExp=3; IntAct=EBI-11574553, EBI-5282479; CC P26022; PRO_0000009136 [O00602]: FCN1; NbExp=7; IntAct=EBI-11574553, EBI-11784425; CC P26022; Q15485: FCN2; NbExp=7; IntAct=EBI-11574553, EBI-7468784; CC P26022; P09038: FGF2; NbExp=16; IntAct=EBI-11574553, EBI-977447; CC P26022; P26022: PTX3; NbExp=17; IntAct=EBI-11574553, EBI-11574553; CC P26022; P98066: TNFAIP6; NbExp=8; IntAct=EBI-11574553, EBI-11700693; CC P26022; P0DTC9: N; Xeno; NbExp=2; IntAct=EBI-11574553, EBI-25475856; CC PRO_0000023545; P08603: CFH; NbExp=8; IntAct=EBI-22114950, EBI-1223708; CC PRO_0000023545; P08603-2: CFH; NbExp=2; IntAct=EBI-22114950, EBI-12684810; CC PRO_0000023545; Q03591: CFHR1; NbExp=5; IntAct=EBI-22114950, EBI-3935840; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- INDUCTION: By IL1B/interleukin-1 beta and TNF. CC -!- PTM: Glycosylated. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X63613; CAA45158.1; -; mRNA. DR EMBL; X63053; CAA44778.1; -; mRNA. DR EMBL; M31166; AAA61234.1; -; mRNA. DR EMBL; DQ207368; ABA64467.1; -; Genomic_DNA. DR EMBL; AK312705; BAG35583.1; -; mRNA. DR EMBL; AC020630; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW78708.1; -; Genomic_DNA. DR EMBL; BC039733; AAH39733.1; -; mRNA. DR CCDS; CCDS3180.1; -. DR PIR; A44323; A44323. DR RefSeq; NP_002843.2; NM_002852.3. DR PDB; 7ZL1; EM; 2.50 A; A/B/C/D/E/F/G/H=18-381. DR PDBsum; 7ZL1; -. DR AlphaFoldDB; P26022; -. DR EMDB; EMD-14774; -. DR EMDB; EMD-14775; -. DR SMR; P26022; -. DR BioGRID; 111770; 74. DR IntAct; P26022; 22. DR STRING; 9606.ENSP00000295927; -. DR UniLectin; P26022; -. DR GlyConnect; 704; 1 N-Linked glycan (1 site). DR GlyCosmos; P26022; 3 sites, 3 glycans. DR GlyGen; P26022; 3 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (2 sites). DR iPTMnet; P26022; -. DR PhosphoSitePlus; P26022; -. DR BioMuta; PTX3; -. DR DMDM; 296452984; -. DR EPD; P26022; -. DR jPOST; P26022; -. DR MassIVE; P26022; -. DR MaxQB; P26022; -. DR PaxDb; 9606-ENSP00000295927; -. DR PeptideAtlas; P26022; -. DR ProteomicsDB; 54310; -. DR Antibodypedia; 33649; 528 antibodies from 37 providers. DR DNASU; 5806; -. DR Ensembl; ENST00000295927.4; ENSP00000295927.3; ENSG00000163661.4. DR GeneID; 5806; -. DR KEGG; hsa:5806; -. DR MANE-Select; ENST00000295927.4; ENSP00000295927.3; NM_002852.4; NP_002843.2. DR UCSC; uc003fbl.5; human. DR AGR; HGNC:9692; -. DR CTD; 5806; -. DR DisGeNET; 5806; -. DR GeneCards; PTX3; -. DR HGNC; HGNC:9692; PTX3. DR HPA; ENSG00000163661; Tissue enhanced (adipose tissue, urinary bladder). DR MIM; 602492; gene. DR neXtProt; NX_P26022; -. DR OpenTargets; ENSG00000163661; -. DR PharmGKB; PA34036; -. DR VEuPathDB; HostDB:ENSG00000163661; -. DR eggNOG; ENOG502QUBX; Eukaryota. DR GeneTree; ENSGT01100000263515; -. DR HOGENOM; CLU_725544_0_0_1; -. DR InParanoid; P26022; -. DR OMA; CDCRREH; -. DR OrthoDB; 4219275at2759; -. DR PhylomeDB; P26022; -. DR TreeFam; TF330208; -. DR PathwayCommons; P26022; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; P26022; -. DR SIGNOR; P26022; -. DR BioGRID-ORCS; 5806; 13 hits in 1145 CRISPR screens. DR ChiTaRS; PTX3; human. DR GeneWiki; PTX3; -. DR GenomeRNAi; 5806; -. DR Pharos; P26022; Tbio. DR PRO; PR:P26022; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P26022; Protein. DR Bgee; ENSG00000163661; Expressed in cartilage tissue and 146 other cell types or tissues. DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome. DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome. DR GO; GO:0001872; F:(1->3)-beta-D-glucan binding; IEA:Ensembl. DR GO; GO:0001849; F:complement component C1q complex binding; IDA:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046790; F:virion binding; IDA:BHF-UCL. DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR GO; GO:0045087; P:innate immune response; IDA:BHF-UCL. DR GO; GO:0044869; P:negative regulation by host of viral exo-alpha-sialidase activity; IDA:BHF-UCL. DR GO; GO:0044871; P:negative regulation by host of viral glycoprotein metabolic process; IDA:BHF-UCL. DR GO; GO:0044793; P:negative regulation by host of viral process; IBA:GO_Central. DR GO; GO:1903016; P:negative regulation of exo-alpha-sialidase activity; IDA:BHF-UCL. DR GO; GO:1903019; P:negative regulation of glycoprotein metabolic process; IDA:BHF-UCL. DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:BHF-UCL. DR GO; GO:0008228; P:opsonization; IEA:Ensembl. DR GO; GO:0001550; P:ovarian cumulus expansion; IEA:Ensembl. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl. DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl. DR GO; GO:0001878; P:response to yeast; IEA:Ensembl. DR CDD; cd00152; PTX; 1. DR Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR006558; LamG-like. DR InterPro; IPR030476; Pentaxin_CS. DR InterPro; IPR001759; Pentraxin-related. DR InterPro; IPR042837; PTX3. DR PANTHER; PTHR46943; PENTRAXIN-RELATED PROTEIN PTX3; 1. DR PANTHER; PTHR46943:SF1; PENTRAXIN-RELATED PROTEIN PTX3; 1. DR Pfam; PF00354; Pentaxin; 1. DR PRINTS; PR00895; PENTAXIN. DR SMART; SM00560; LamGL; 1. DR SMART; SM00159; PTX; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS00289; PTX_1; 1. DR PROSITE; PS51828; PTX_2; 1. DR Genevisible; P26022; HS. PE 1: Evidence at protein level; KW 3D-structure; Coiled coil; Disulfide bond; Glycoprotein; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..17 FT /evidence="ECO:0000255" FT CHAIN 18..381 FT /note="Pentraxin-related protein PTX3" FT /id="PRO_0000023545" FT DOMAIN 179..381 FT /note="Pentraxin (PTX)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172" FT COILED 74..101 FT /evidence="ECO:0000255" FT COILED 143..167 FT /evidence="ECO:0000255" FT CARBOHYD 220 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 47 FT /note="Interchain" FT /evidence="ECO:0000269|PubMed:18223257" FT DISULFID 49 FT /note="Interchain" FT /evidence="ECO:0000269|PubMed:18223257" FT DISULFID 103 FT /note="Interchain" FT /evidence="ECO:0000269|PubMed:18223257" FT DISULFID 179..357 FT /evidence="ECO:0000269|PubMed:18223257" FT DISULFID 210..271 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172, FT ECO:0000269|PubMed:18223257" FT DISULFID 317 FT /note="Interchain" FT /evidence="ECO:0000269|PubMed:18223257" FT DISULFID 318 FT /note="Interchain" FT /evidence="ECO:0000269|PubMed:18223257" FT VARIANT 39 FT /note="H -> Q (in dbSNP:rs34655398)" FT /id="VAR_043140" FT VARIANT 48 FT /note="A -> D (in dbSNP:rs3816527)" FT /evidence="ECO:0000269|PubMed:1429570, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7679696, FT ECO:0000269|PubMed:8131794" FT /id="VAR_043141" FT VARIANT 290 FT /note="A -> V (in dbSNP:rs35415718)" FT /id="VAR_043142" FT VARIANT 313 FT /note="E -> K (in dbSNP:rs4478039)" FT /id="VAR_043143" FT CONFLICT 202 FT /note="M -> L (in Ref. 3; AAA61234)" FT /evidence="ECO:0000305" FT HELIX 168..172 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 176..178 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 182..185 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 193..197 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 204..216 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 222..228 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 235..241 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 244..251 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 254..260 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 268..275 FT /evidence="ECO:0007829|PDB:7ZL1" FT HELIX 276..278 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 280..285 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 288..297 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 307..312 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 317..319 FT /evidence="ECO:0007829|PDB:7ZL1" FT HELIX 325..327 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 331..341 FT /evidence="ECO:0007829|PDB:7ZL1" FT HELIX 345..351 FT /evidence="ECO:0007829|PDB:7ZL1" FT HELIX 356..358 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 362..364 FT /evidence="ECO:0007829|PDB:7ZL1" FT TURN 366..368 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 369..374 FT /evidence="ECO:0007829|PDB:7ZL1" FT STRAND 378..380 FT /evidence="ECO:0007829|PDB:7ZL1" SQ SEQUENCE 381 AA; 41976 MW; 09BCE02E2A62D62A CRC64; MHLLAILFCA LWSAVLAENS DDYDLMYVNL DNEIDNGLHP TEDPTPCACG QEHSEWDKLF IMLENSQMRE RMLLQATDDV LRGELQRLRE ELGRLAESLA RPCAPGAPAE ARLTSALDEL LQATRDAGRR LARMEGAEAQ RPEEAGRALA AVLEELRQTR ADLHAVQGWA ARSWLPAGCE TAILFPMRSK KIFGSVHPVR PMRLESFSAC IWVKATDVLN KTILFSYGTK RNPYEIQLYL SYQSIVFVVG GEENKLVAEA MVSLGRWTHL CGTWNSEEGL TSLWVNGELA ATTVEMATGH IVPEGGILQI GQEKNGCCVG GGFDETLAFS GRLTGFNIWD SVLSNEEIRE TGGAESCHIR GNIVGWGVTE IQPHGGAQYV S //