ID FHR1_HUMAN Reviewed; 330 AA. AC Q03591; A8K465; Q3B774; Q9UJ17; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 2. DT 27-MAR-2024, entry version 186. DE RecName: Full=Complement factor H-related protein 1; DE Short=FHR-1; DE AltName: Full=H factor-like protein 1; DE Short=FHL-1 {ECO:0000303|PubMed:23204165}; DE Short=H-factor-like 1; DE AltName: Full=H36; DE Flags: Precursor; GN Name=CFHR1; Synonyms=CFHL, CFHL1, CFHL1P, CFHR1P, FHR1, HFL1, HFL2; 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 VARIANTS TYR-157; VAL-159 AND GLN-175. RC TISSUE=Liver; RX PubMed=1826708; RA Estaller C., Koistinen V., Schwaeble W., Dierich M.P., Weiss E.H.; RT "Cloning of the 1.4-kb mRNA species of human complement factor H reveals a RT novel member of the short consensus repeat family related to the carboxy RT terminal of the classical 150-kDa molecule."; RL J. Immunol. 146:3190-3196(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10781834; DOI=10.1016/s0161-5890(00)00024-9; RA Male D.A., Ormsby R.J., Ranganathan S., Giannakis E., Gordon D.L.; RT "Complement factor H: sequence analysis of 221 kb of human genomic DNA RT containing the entire fH, fHR-1 and fHR-3 genes."; RL Mol. Immunol. 37:41-52(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-157; VAL-159 AND RP GLN-175. RC TISSUE=Liver; 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 GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver, and Skeletal muscle; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-330, AND VARIANTS TYR-157; VAL-159 AND RP GLN-175. RX PubMed=1711047; DOI=10.1016/s0021-9258(18)99058-7; RA Skerka C., Horstmann R.D., Zipfel P.F.; RT "Molecular cloning of a human serum protein structurally related to RT complement factor H."; RL J. Biol. Chem. 266:12015-12020(1991). RN [7] RP STRUCTURE OF CARBOHYDRATES. RX PubMed=1825108; RA Timmann C., Leippe M., Horstmann R.D.; RT "Two major serum components antigenically related to complement factor H RT are different glycosylation forms of a single protein with no factor H-like RT complement regulatory functions."; RL J. Immunol. 146:1265-1270(1991). RN [8] RP REVIEW. RX PubMed=8172644; DOI=10.1016/0167-5699(94)90155-4; RA Zipfel P.F., Skerka C.; RT "Complement factor H and related proteins: an expanding family of RT complement-regulatory proteins?"; RL Immunol. Today 15:121-126(1994). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126 AND ASN-194. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [10] RP INVOLVEMENT IN AHUS1. RX PubMed=17367211; DOI=10.1371/journal.pgen.0030041; RA Zipfel P.F., Edey M., Heinen S., Jozsi M., Richter H., Misselwitz J., RA Hoppe B., Routledge D., Strain L., Hughes A.E., Goodship J.A., Licht C., RA Goodship T.H., Skerka C.; RT "Deletion of complement factor H-related genes CFHR1 and CFHR3 is RT associated with atypical hemolytic uremic syndrome."; RL PLoS Genet. 3:E41-E41(2007). RN [11] RP INVOLVEMENT IN AHUS1. RX PubMed=18006700; DOI=10.1182/blood-2007-09-109876; RA Jozsi M., Licht C., Strobel S., Zipfel S.L., Richter H., Heinen S., RA Zipfel P.F., Skerka C.; RT "Factor H autoantibodies in atypical hemolytic uremic syndrome correlate RT with CFHR1/CFHR3 deficiency."; RL Blood 111:1512-1514(2008). RN [12] RP INTERACTION WITH C.ALBICANS GPD2 (MICROBIAL INFECTION). RX PubMed=23204165; DOI=10.1093/infdis/jis718; RA Luo S., Hoffmann R., Skerka C., Zipfel P.F.; RT "Glycerol-3-phosphate dehydrogenase 2 is a novel factor H-, factor H-like RT protein 1-, and plasminogen-binding surface protein of Candida albicans."; RL J. Infect. Dis. 207:594-603(2013). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 19-143, FUNCTION, SUBUNIT, AND RP DISULFIDE BONDS. RX PubMed=23487775; DOI=10.1073/pnas.1219260110; RA Goicoechea de Jorge E., Caesar J.J., Malik T.H., Patel M., Colledge M., RA Johnson S., Hakobyan S., Morgan B.P., Harris C.L., Pickering M.C., RA Lea S.M.; RT "Dimerization of complement factor H-related proteins modulates complement RT activation in vivo."; RL Proc. Natl. Acad. Sci. U.S.A. 110:4685-4690(2013). CC -!- FUNCTION: Involved in complement regulation. The dimerized forms have CC avidity for tissue-bound complement fragments and efficiently compete CC with the physiological complement inhibitor CFH. Can associate with CC lipoproteins and may play a role in lipid metabolism. CC {ECO:0000269|PubMed:23487775}. CC -!- SUBUNIT: Head-to-tail homodimer and heterodimer with CFHR2 or CFHR5. CC {ECO:0000269|PubMed:23487775}. CC -!- SUBUNIT: (Microbial infection) Interacts with C.albicans GPD2; the CC interaction is direct and leads to the degradation of C3. CC {ECO:0000269|PubMed:23204165}. CC -!- INTERACTION: CC Q03591; Q9UHX3: ADGRE2; NbExp=5; IntAct=EBI-3935840, EBI-11277970; CC Q03591; P01031: C5; NbExp=3; IntAct=EBI-3935840, EBI-8558308; CC Q03591; Q03591: CFHR1; NbExp=6; IntAct=EBI-3935840, EBI-3935840; CC Q03591; P36980: CFHR2; NbExp=4; IntAct=EBI-3935840, EBI-21976709; CC Q03591; Q9BXR6: CFHR5; NbExp=3; IntAct=EBI-3935840, EBI-11579371; CC Q03591; P02741: CRP; NbExp=10; IntAct=EBI-3935840, EBI-1395983; CC Q03591; PRO_0000023545 [P26022]: PTX3; NbExp=5; IntAct=EBI-3935840, EBI-22114950; CC PRO_0000005896; P01024: C3; NbExp=2; IntAct=EBI-22118464, EBI-905851; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- PTM: N-glycosylated. Two forms are observed; one with a single side CC chain and the other with two. {ECO:0000269|PubMed:16335952}. CC -!- DISEASE: Hemolytic uremic syndrome, atypical, 1 (AHUS1) [MIM:235400]: CC An atypical form of hemolytic uremic syndrome. It is a complex genetic CC disease characterized by microangiopathic hemolytic anemia, CC thrombocytopenia, renal failure and absence of episodes of CC enterocolitis and diarrhea. In contrast to typical hemolytic uremic CC syndrome, atypical forms have a poorer prognosis, with higher death CC rates and frequent progression to end-stage renal disease. CC {ECO:0000269|PubMed:17367211}. Note=Disease susceptibility is CC associated with variants affecting the gene represented in this entry. CC A deletion encompassing CFHR1 and CFHR3 is associated with an increased CC risk of atypical hemolytic uremic syndrome, likely due to a defective CC regulation of complement activation (PubMed:17367211). Some patients CC carrying the deletion have serum anti-CFH autoantibodies CC (PubMed:18006700). {ECO:0000269|PubMed:17367211, CC ECO:0000269|PubMed:18006700}. 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; M65292; AAA35946.1; -; mRNA. DR EMBL; M65293; AAA35947.1; -; mRNA. DR EMBL; AK290830; BAF83519.1; -; mRNA. DR EMBL; AL049741; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC016755; AAH16755.1; -; mRNA. DR EMBL; BC107771; AAI07772.1; -; mRNA. DR EMBL; X56209; CAA39666.1; -; mRNA. DR CCDS; CCDS1386.1; -. DR PIR; I56100; I56100. DR RefSeq; NP_002104.2; NM_002113.2. DR PDB; 3ZD2; X-ray; 1.99 A; A/B=19-143. DR PDB; 4MUC; X-ray; 2.90 A; A/B=205-329. DR PDBsum; 3ZD2; -. DR PDBsum; 4MUC; -. DR AlphaFoldDB; Q03591; -. DR SMR; Q03591; -. DR BioGRID; 109326; 5. DR IntAct; Q03591; 14. DR MINT; Q03591; -. DR STRING; 9606.ENSP00000314299; -. DR GlyConnect; 1152; 11 N-Linked glycans (2 sites). DR GlyCosmos; Q03591; 2 sites, 10 glycans. DR GlyGen; Q03591; 2 sites, 11 N-linked glycans (2 sites). DR iPTMnet; Q03591; -. DR PhosphoSitePlus; Q03591; -. DR BioMuta; CFHR1; -. DR DMDM; 218512041; -. DR EPD; Q03591; -. DR jPOST; Q03591; -. DR MassIVE; Q03591; -. DR MaxQB; Q03591; -. DR PaxDb; 9606-ENSP00000314299; -. DR PeptideAtlas; Q03591; -. DR ProteomicsDB; 58217; -. DR Pumba; Q03591; -. DR Antibodypedia; 34881; 291 antibodies from 29 providers. DR DNASU; 3078; -. DR Ensembl; ENST00000320493.10; ENSP00000314299.5; ENSG00000244414.8. DR GeneID; 3078; -. DR KEGG; hsa:3078; -. DR MANE-Select; ENST00000320493.10; ENSP00000314299.5; NM_002113.3; NP_002104.2. DR UCSC; uc001gtn.4; human. DR AGR; HGNC:4888; -. DR CTD; 3078; -. DR DisGeNET; 3078; -. DR GeneCards; CFHR1; -. DR GeneReviews; CFHR1; -. DR HGNC; HGNC:4888; CFHR1. DR HPA; ENSG00000244414; Tissue enriched (liver). DR MalaCards; CFHR1; -. DR MIM; 134371; gene. DR MIM; 235400; phenotype. DR neXtProt; NX_Q03591; -. DR OpenTargets; ENSG00000244414; -. DR Orphanet; 93581; Atypical hemolytic uremic syndrome with anti-factor H antibodies. DR Orphanet; 329931; C3 glomerulonephritis. DR Orphanet; 93571; Dense deposit disease. DR PharmGKB; PA29265; -. DR VEuPathDB; HostDB:ENSG00000244414; -. DR eggNOG; ENOG502RTVV; Eukaryota. DR GeneTree; ENSGT00940000163634; -. DR InParanoid; Q03591; -. DR OMA; HILSRQM; -. DR PhylomeDB; Q03591; -. DR TreeFam; TF326157; -. DR PathwayCommons; Q03591; -. DR Reactome; R-HSA-977606; Regulation of Complement cascade. DR SignaLink; Q03591; -. DR SIGNOR; Q03591; -. DR BioGRID-ORCS; 3078; 7 hits in 1038 CRISPR screens. DR ChiTaRS; CFHR1; human. DR GeneWiki; CFHR1; -. DR GenomeRNAi; 3078; -. DR Pharos; Q03591; Tbio. DR PRO; PR:Q03591; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q03591; Protein. DR Bgee; ENSG00000244414; Expressed in right lobe of liver and 88 other cell types or tissues. DR ExpressionAtlas; Q03591; baseline and differential. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0001851; F:complement component C3b binding; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0006956; P:complement activation; IBA:GO_Central. DR GO; GO:0051838; P:cytolysis by host of symbiont cells; IMP:UniProtKB. DR GO; GO:0032091; P:negative regulation of protein binding; IMP:UniProtKB. DR CDD; cd00033; CCP; 3. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 5. DR InterPro; IPR035976; Sushi/SCR/CCP_sf. DR InterPro; IPR000436; Sushi_SCR_CCP_dom. DR PANTHER; PTHR45785:SF7; COMPLEMENT FACTOR H; 1. DR PANTHER; PTHR45785; COMPLEMENT FACTOR H-RELATED; 1. DR Pfam; PF00084; Sushi; 5. DR SMART; SM00032; CCP; 5. DR SUPFAM; SSF57535; Complement control module/SCR domain; 5. DR PROSITE; PS50923; SUSHI; 4. DR Genevisible; Q03591; HS. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Glycoprotein; Hemolytic uremic syndrome; KW Reference proteome; Repeat; Secreted; Signal; Sushi. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..330 FT /note="Complement factor H-related protein 1" FT /id="PRO_0000005896" FT DOMAIN 22..84 FT /note="Sushi 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 85..142 FT /note="Sushi 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 145..203 FT /note="Sushi 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 206..264 FT /note="Sushi 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 273..329 FT /note="Sushi 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT CARBOHYD 126 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 194 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT DISULFID 23..72 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302, FT ECO:0000269|PubMed:23487775" FT DISULFID 55..83 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302, FT ECO:0000269|PubMed:23487775" FT DISULFID 87..129 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302, FT ECO:0000269|PubMed:23487775" FT DISULFID 114..140 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302, FT ECO:0000269|PubMed:23487775" FT DISULFID 147..190 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 176..201 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 208..251 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 237..262 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 266..317 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 300..327 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT VARIANT 157 FT /note="H -> Y (in dbSNP:rs425757)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:1711047, ECO:0000269|PubMed:1826708" FT /id="VAR_001980" FT VARIANT 159 FT /note="L -> V (in dbSNP:rs410232)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:1711047, ECO:0000269|PubMed:1826708" FT /id="VAR_001981" FT VARIANT 175 FT /note="E -> Q (in dbSNP:rs388862)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:1711047, ECO:0000269|PubMed:1826708" FT /id="VAR_001982" FT VARIANT 296 FT /note="A -> V (in dbSNP:rs16840561)" FT /id="VAR_048816" FT CONFLICT 71 FT /note="T -> N (in Ref. 6; CAA39666)" FT /evidence="ECO:0000305" FT STRAND 21..24 FT /evidence="ECO:0007829|PDB:3ZD2" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:3ZD2" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:3ZD2" FT STRAND 44..46 FT /evidence="ECO:0007829|PDB:3ZD2" FT STRAND 50..55 FT /evidence="ECO:0007829|PDB:3ZD2" FT STRAND 66..73 FT /evidence="ECO:0007829|PDB:3ZD2" FT STRAND 76..79 FT /evidence="ECO:0007829|PDB:3ZD2" FT STRAND 84..87 FT /evidence="ECO:0007829|PDB:3ZD2" FT TURN 98..101 FT /evidence="ECO:0007829|PDB:3ZD2" FT STRAND 125..130 FT /evidence="ECO:0007829|PDB:3ZD2" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:3ZD2" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:4MUC" FT STRAND 232..237 FT /evidence="ECO:0007829|PDB:4MUC" FT STRAND 242..245 FT /evidence="ECO:0007829|PDB:4MUC" FT STRAND 247..252 FT /evidence="ECO:0007829|PDB:4MUC" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:4MUC" FT HELIX 270..275 FT /evidence="ECO:0007829|PDB:4MUC" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:4MUC" FT HELIX 282..284 FT /evidence="ECO:0007829|PDB:4MUC" FT STRAND 295..300 FT /evidence="ECO:0007829|PDB:4MUC" FT STRAND 313..318 FT /evidence="ECO:0007829|PDB:4MUC" SQ SEQUENCE 330 AA; 37651 MW; C0A1B38B8B34B6EF CRC64; MWLLVSVILI SRISSVGGEA TFCDFPKINH GILYDEEKYK PFSQVPTGEV FYYSCEYNFV SPSKSFWTRI TCTEEGWSPT PKCLRLCFFP FVENGHSESS GQTHLEGDTV QIICNTGYRL QNNENNISCV ERGWSTPPKC RSTDTSCVNP PTVQNAHILS RQMSKYPSGE RVRYECRSPY EMFGDEEVMC LNGNWTEPPQ CKDSTGKCGP PPPIDNGDIT SFPLSVYAPA SSVEYQCQNL YQLEGNKRIT CRNGQWSEPP KCLHPCVISR EIMENYNIAL RWTAKQKLYL RTGESAEFVC KRGYRLSSRS HTLRTTCWDG KLEYPTCAKR //