CFAH_MOUSE
ID CFAH_MOUSE Reviewed; 1234 AA.
AC P06909; Q6NZK3;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Complement factor H;
DE AltName: Full=Protein beta-1-H;
DE Flags: Precursor;
GN Name=Cfh; Synonyms=Hf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2940596; DOI=10.1073/pnas.83.11.3963;
RA Kristensen T., Tack B.F.;
RT "Murine protein H is comprised of 20 repeating units, 61 amino acids in
RT length.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3963-3967(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-19.
RC STRAIN=BALB/cJ;
RX PubMed=2533512; DOI=10.1021/bi00452a002;
RA Munoz-Canoves P., Tack B.F., Vik D.P.;
RT "Analysis of complement factor H mRNA expression: dexamethasone and IFN-
RT gamma increase the level of H in L cells.";
RL Biochemistry 28:9891-9897(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-18.
RX PubMed=2136885;
RA Natsuume-Sakai S., Nonaka M., Nonaka M., Harada Y.N., Shreffler D.C.,
RA Moriwaki K.;
RT "Demonstration of an unusual allelic variation of mouse factor H by the
RT complete cDNA sequence of the H.2 allotype.";
RL J. Immunol. 144:358-362(1990).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-773 AND ASN-1061.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-773; ASN-801; ASN-1030;
RP ASN-1061 AND ASN-1225.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=30107932; DOI=10.1016/j.imbio.2018.07.023;
RA Alexander J.J., Sankaran J.S., Seldeen K.L., Thiyagarajan R., Jacob A.,
RA Quigg R.J., Troen B.R., Judex S.;
RT "Absence of complement factor H alters bone architecture and dynamics.";
RL Immunobiology 223:761-771(2018).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 321-444.
RX PubMed=23133374; DOI=10.1371/journal.ppat.1002981;
RA Johnson S., Tan L., van der Veen S., Caesar J., Goicoechea De Jorge E.,
RA Harding R.J., Bai X., Exley R.M., Ward P.N., Ruivo N., Trivedi K.,
RA Cumber E., Jones R., Newham L., Staunton D., Ufret-Vincenty R., Borrow R.,
RA Pickering M.C., Lea S.M., Tang C.M.;
RT "Design and evaluation of meningococcal vaccines through structure-based
RT modification of host and pathogen molecules.";
RL PLoS Pathog. 8:E1002981-E1002981(2012).
CC -!- FUNCTION: Glycoprotein that plays an essential role in maintaining a
CC well-balanced immune response by modulating complement activation. Acts
CC as a soluble inhibitor of complement, where its binding to self markers
CC such as glycan structures prevents complement activation and
CC amplification on cell surfaces. Accelerates the decay of the complement
CC alternative pathway (AP) C3 convertase C3bBb, thus preventing local
CC formation of more C3b, the central player of the complement
CC amplification loop. As a cofactor of the serine protease factor I, CFH
CC also regulates proteolytic degradation of already-deposited C3b. In
CC addition, mediates several cellular responses through interaction with
CC specific receptors. For example, interacts with CR3/ITGAM receptor and
CC thereby mediates the adhesion of human neutrophils to different
CC pathogens. In turn, these pathogens are phagocytosed and destroyed.
CC {ECO:0000250|UniProtKB:P08603}.
CC -!- SUBUNIT: Homodimer. Forms also homooligomers. Interacts with complement
CC protein C3b; this interaction inhibits complement activation. Interacts
CC with complement protein C3d. Interacts with CR3/ITGAM; this interaction
CC mediates adhesion of neutrophils to pathogens leading to pathogen
CC clearance. {ECO:0000250|UniProtKB:P08603}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P08603}.
CC -!- TISSUE SPECIFICITY: CFH is one of the most abundant complement
CC components in blood where the liver is the major source of CFH protein
CC in vivo. in addition, CFH is secreted by additional cell types
CC including monocytes, fibroblasts, or endothelial cells.
CC {ECO:0000250|UniProtKB:P08603}.
CC -!- DOMAIN: Sushi 1-3 domain represents the minimal unit capable of
CC cofactor activity. The property to discriminate self surfaces from non-
CC self surfaces depends on the C-terminal region made of Sushis 19-20.
CC {ECO:0000250|UniProtKB:P08603}.
CC -!- PTM: Sulfated on tyrosine residues. {ECO:0000250|UniProtKB:P08603}.
CC -!- POLYMORPHISM: Two codominant alleles of factor H are present in mice.
CC -!- DISRUPTION PHENOTYPE: The lack of CFH alters the microarchitecture of
CC bone and affects osteoblast and osteoclast dynamics.
CC {ECO:0000269|PubMed:30107932}.
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DR EMBL; M12660; AAA37759.1; -; mRNA.
DR EMBL; AC161408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC066092; AAH66092.1; -; mRNA.
DR EMBL; J02891; AAA37795.1; -; mRNA.
DR EMBL; AH001909; AAA37762.1; -; mRNA.
DR PIR; A26154; NBMSH.
DR RefSeq; NP_034018.2; NM_009888.3.
DR PDB; 2YBY; X-ray; 1.58 A; A=321-444.
DR PDBsum; 2YBY; -.
DR AlphaFoldDB; P06909; -.
DR SMR; P06909; -.
DR BioGRID; 198682; 1.
DR STRING; 10090.ENSMUSP00000107607; -.
DR GlyConnect; 817; 2 N-Linked glycans (2 sites).
DR GlyGen; P06909; 7 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; P06909; -.
DR PhosphoSitePlus; P06909; -.
DR SwissPalm; P06909; -.
DR CPTAC; non-CPTAC-3900; -.
DR CPTAC; non-CPTAC-5588; -.
DR jPOST; P06909; -.
DR PaxDb; P06909; -.
DR PRIDE; P06909; -.
DR ProteomicsDB; 281396; -.
DR DNASU; 12628; -.
DR Ensembl; ENSMUST00000066859; ENSMUSP00000066677; ENSMUSG00000026365.
DR GeneID; 12628; -.
DR KEGG; mmu:12628; -.
DR CTD; 3075; -.
DR MGI; MGI:88385; Cfh.
DR VEuPathDB; HostDB:ENSMUSG00000026365; -.
DR eggNOG; ENOG502QVSB; Eukaryota.
DR GeneTree; ENSGT00940000164315; -.
DR HOGENOM; CLU_003511_0_0_1; -.
DR InParanoid; P06909; -.
DR OrthoDB; 296899at2759; -.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 12628; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cfh; mouse.
DR PRO; PR:P06909; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P06909; protein.
DR Bgee; ENSMUSG00000026365; Expressed in diaphysis of femur and 263 other tissues.
DR ExpressionAtlas; P06909; baseline and differential.
DR Genevisible; P06909; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:MGI.
DR GO; GO:0001851; F:complement component C3b binding; IPI:MGI.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0001905; P:activation of membrane attack complex; IMP:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0046034; P:ATP metabolic process; IMP:MGI.
DR GO; GO:0006956; P:complement activation; IDA:MGI.
DR GO; GO:0006957; P:complement activation, alternative pathway; IMP:MGI.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0032835; P:glomerulus development; IMP:MGI.
DR GO; GO:0006955; P:immune response; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0032042; P:mitochondrial DNA metabolic process; IMP:MGI.
DR GO; GO:0140053; P:mitochondrial gene expression; IMP:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0070487; P:monocyte aggregation; IMP:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0051640; P:organelle localization; IMP:MGI.
DR GO; GO:0046530; P:photoreceptor cell differentiation; IMP:MGI.
DR GO; GO:0070527; P:platelet aggregation; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0030449; P:regulation of complement activation; IMP:MGI.
DR GO; GO:0030451; P:regulation of complement activation, alternative pathway; ISO:MGI.
DR GO; GO:1903659; P:regulation of complement-dependent cytotoxicity; ISO:MGI.
DR GO; GO:0034097; P:response to cytokine; IDA:MGI.
DR GO; GO:0002021; P:response to dietary excess; IMP:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0003406; P:retinal pigment epithelium development; IMP:MGI.
DR GO; GO:0046548; P:retinal rod cell development; IMP:MGI.
DR GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; IMP:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR CDD; cd00033; CCP; 16.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 16.
DR SMART; SM00032; CCP; 20.
DR SUPFAM; SSF57535; SSF57535; 18.
DR PROSITE; PS50923; SUSHI; 18.
PE 1: Evidence at protein level;
KW 3D-structure; Complement alternate pathway; Disulfide bond; Glycoprotein;
KW Immunity; Innate immunity; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal; Sulfation; Sushi.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..1234
FT /note="Complement factor H"
FT /id="PRO_0000005895"
FT DOMAIN 19..82
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 83..143
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 144..207
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 208..264
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 265..322
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 324..386
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 387..444
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 446..507
FT /note="Sushi 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 508..566
FT /note="Sushi 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 567..624
FT /note="Sushi 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 627..685
FT /note="Sushi 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 688..745
FT /note="Sushi 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 750..804
FT /note="Sushi 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 806..863
FT /note="Sushi 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 865..933
FT /note="Sushi 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 934..991
FT /note="Sushi 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 992..1050
FT /note="Sushi 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1051..1109
FT /note="Sushi 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1112..1170
FT /note="Sushi 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1171..1234
FT /note="Sushi 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 872..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 1030
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 1061
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 1225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT DISULFID 21..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 52..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 85..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 114..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 146..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 178..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 210..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 237..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 267..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 294..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 325..374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 357..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 389..431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 416..442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 448..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 477..505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 509..553
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 536..564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 569..610
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 597..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 629..672
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 658..683
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 690..732
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 718..743
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 752..791
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 780..802
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 808..850
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 836..861
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 867..920
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 906..931
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 936..978
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 964..989
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 994..1037
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1023..1048
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1053..1096
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1082..1107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1114..1157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1143..1168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1172..1223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1206..1233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CONFLICT 1158
FT /note="R -> T (in Ref. 1; AAA37759)"
FT /evidence="ECO:0000305"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:2YBY"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:2YBY"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:2YBY"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:2YBY"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:2YBY"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:2YBY"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:2YBY"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:2YBY"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:2YBY"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:2YBY"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:2YBY"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:2YBY"
SQ SEQUENCE 1234 AA; 139138 MW; 0A5722F34620C9F0 CRC64;
MRLSARIIWL ILWTVCAAED CKGPPPRENS EILSGSWSEQ LYPEGTQATY KCRPGYRTLG
TIVKVCKNGK WVASNPSRIC RKKPCGHPGD TPFGSFRLAV GSQFEFGAKV VYTCDDGYQL
LGEIDYRECG ADGWINDIPL CEVVKCLPVT ELENGRIVSG AAETDQEYYF GQVVRFECNS
GFKIEGHKEI HCSENGLWSN EKPRCVEILC TPPRVENGDG INVKPVYKEN ERYHYKCKHG
YVPKERGDAV CTGSGWSSQP FCEEKRCSPP YILNGIYTPH RIIHRSDDEI RYECNYGFYP
VTGSTVSKCT PTGWIPVPRC TLKPCEFPQF KYGRLYYEES LRPNFPVSIG NKYSYKCDNG
FSPPSGYSWD YLRCTAQGWE PEVPCVRKCV FHYVENGDSA YWEKVYVQGQ SLKVQCYNGY
SLQNGQDTMT CTENGWSPPP KCIRIKTCSA SDIHIDNGFL SESSSIYALN RETSYRCKQG
YVTNTGEISG SITCLQNGWS PQPSCIKSCD MPVFENSITK NTRTWFKLND KLDYECLVGF
ENEYKHTKGS ITCTYYGWSD TPSCYERECS VPTLDRKLVV SPRKEKYRVG DLLEFSCHSG
HRVGPDSVQC YHFGWSPGFP TCKGQVASCA PPLEILNGEI NGAKKVEYSH GEVVKYDCKP
RFLLKGPNKI QCVDGNWTTL PVCIEEERTC GDIPELEHGS AKCSVPPYHH GDSVEFICEE
NFTMIGHGSV SCISGKWTQL PKCVATDQLE KCRVLKSTGI EAIKPKLTEF THNSTMDYKC
RDKQEYERSI CINGKWDPEP NCTSKTSCPP PPQIPNTQVI ETTVKYLDGE KLSVLCQDNY
LTQDSEEMVC KDGRWQSLPR CIEKIPCSQP PTIEHGSINL PRSSEERRDS IESSSHEHGT
TFSYVCDDGF RIPEENRITC YMGKWSTPPR CVGLPCGPPP SIPLGTVSLE LESYQHGEEV
TYHCSTGFGI DGPAFIICEG GKWSDPPKCI KTDCDVLPTV KNAIIRGKSK KSYRTGEQVT
FRCQSPYQMN GSDTVTCVNS RWIGQPVCKD NSCVDPPHVP NATIVTRTKN KYLHGDRVRY
ECNKPLELFG QVEVMCENGI WTEKPKCRDS TGKCGPPPPI DNGDITSLSL PVYEPLSSVE
YQCQKYYLLK GKKTITCRNG KWSEPPTCLH ACVIPENIME SHNIILKWRH TEKIYSHSGE
DIEFGCKYGY YKARDSPPFR TKCINGTINY PTCV
