FHR1_HUMAN
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 03-AUG-2022, entry version 178.
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]: An
CC 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}.
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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 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; Q03591; -.
DR PeptideAtlas; Q03591; -.
DR PRIDE; Q03591; -.
DR ProteomicsDB; 58217; -.
DR Antibodypedia; 34881; 258 antibodies from 29 providers.
DR DNASU; 3078; -.
DR Ensembl; ENST00000320493.10; ENSP00000314299.5; ENSG00000244414.7.
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 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 OrthoDB; 845963at2759; -.
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 977 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 87 other tissues.
DR ExpressionAtlas; Q03591; baseline and differential.
DR Genevisible; Q03591; HS.
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 InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 5.
DR SMART; SM00032; CCP; 5.
DR SUPFAM; SSF57535; SSF57535; 5.
DR PROSITE; PS50923; SUSHI; 4.
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
