HORN_HUMAN
ID HORN_HUMAN Reviewed; 2850 AA.
AC Q86YZ3; Q5DT20; Q5U1F4;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Hornerin;
GN Name=HRNR; Synonyms=S100A18;
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 TISSUE SPECIFICITY.
RC TISSUE=Skin;
RX PubMed=15507446; DOI=10.1074/jbc.m409026200;
RA Takaishi M., Makino T., Morohashi M., Huh N.-H.;
RT "Identification of human hornerin and its expression in regenerating and
RT psoriatic skin.";
RL J. Biol. Chem. 280:4696-4703(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-85.
RC TISSUE=Skin;
RA Wu Z., Bartels J., Schroeder J.M.;
RT "Human intermediate filament-associated protein family.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, TRANSGLUTAMINATION, AND TISSUE SPECIFICITY.
RX PubMed=21282207; DOI=10.1096/fj.10-168658;
RA Henry J., Hsu C.Y., Haftek M., Nachat R., de Koning H.D.,
RA Gardinal-Galera I., Hitomi K., Balica S., Jean-Decoster C., Schmitt A.M.,
RA Paul C., Serre G., Simon M.;
RT "Hornerin is a component of the epidermal cornified cell envelopes.";
RL FASEB J. 25:1567-1576(2011).
RN [9]
RP INDUCTION BY UV-B.
RX PubMed=23751202; DOI=10.1016/j.acthis.2013.05.001;
RA Makino T., Yamakoshi T., Mizawa M., Shimizu T.;
RT "Ultraviolet B irradiation induces the expression of hornerin in
RT xenotransplanted human skin.";
RL Acta Histochem. 116:20-24(2014).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659; SER-661; SER-993;
RP SER-1008; SER-1463; SER-1478; SER-1712; SER-1714; SER-1829; SER-1831;
RP SER-1933; SER-1948; SER-2299; SER-2301; SER-2403; SER-2418; SER-2652 AND
RP SER-2654, AND 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).
CC -!- FUNCTION: Component of the epidermal cornified cell envelopes.
CC {ECO:0000269|PubMed:21282207}.
CC -!- INTERACTION:
CC Q86YZ3; Q93009: USP7; NbExp=2; IntAct=EBI-1047017, EBI-302474;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule
CC {ECO:0000269|PubMed:21282207}. Note=Found in keratohyalin granules in
CC the granular cells of the epidermis.
CC -!- TISSUE SPECIFICITY: Expressed in cornified epidermis, psoriatic and
CC regenerating skin after wounding. Found in the upper granular layer and
CC in the entire cornified layer of epidermis.
CC {ECO:0000269|PubMed:15507446, ECO:0000269|PubMed:21282207}.
CC -!- INDUCTION: By UV-B irradiation. {ECO:0000269|PubMed:23751202}.
CC -!- PTM: Processed during the process of epidermal differentiation.
CC {ECO:0000250}.
CC -!- PTM: Forms covalent cross-links mediated by transglutaminase TGM3,
CC between glutamine and the epsilon-amino group of lysine residues (in
CC vitro). {ECO:0000269|PubMed:21282207}.
CC -!- SIMILARITY: Belongs to the S100-fused protein family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the S-100 family.
CC {ECO:0000305}.
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DR EMBL; AB104446; BAC57496.1; -; mRNA.
DR EMBL; BR000036; FAA00004.1; -; mRNA.
DR EMBL; AY396741; AAR91619.1; -; mRNA.
DR EMBL; AL589986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30859.1; -.
DR RefSeq; NP_001009931.1; NM_001009931.2.
DR SMR; Q86YZ3; -.
DR BioGRID; 132814; 113.
DR IntAct; Q86YZ3; 35.
DR MINT; Q86YZ3; -.
DR STRING; 9606.ENSP00000357791; -.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR GlyGen; Q86YZ3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86YZ3; -.
DR PhosphoSitePlus; Q86YZ3; -.
DR BioMuta; HRNR; -.
DR DMDM; 45476906; -.
DR UCD-2DPAGE; Q86YZ3; -.
DR jPOST; Q86YZ3; -.
DR MassIVE; Q86YZ3; -.
DR PaxDb; Q86YZ3; -.
DR PeptideAtlas; Q86YZ3; -.
DR PRIDE; Q86YZ3; -.
DR ProteomicsDB; 70490; -.
DR Antibodypedia; 34085; 93 antibodies from 20 providers.
DR DNASU; 388697; -.
DR Ensembl; ENST00000368801.4; ENSP00000357791.3; ENSG00000197915.7.
DR GeneID; 388697; -.
DR KEGG; hsa:388697; -.
DR MANE-Select; ENST00000368801.4; ENSP00000357791.3; NM_001009931.3; NP_001009931.1.
DR UCSC; uc001ezt.3; human.
DR CTD; 388697; -.
DR DisGeNET; 388697; -.
DR GeneCards; HRNR; -.
DR HGNC; HGNC:20846; HRNR.
DR HPA; ENSG00000197915; Tissue enhanced (brain).
DR MIM; 616293; gene.
DR neXtProt; NX_Q86YZ3; -.
DR OpenTargets; ENSG00000197915; -.
DR PharmGKB; PA134936141; -.
DR VEuPathDB; HostDB:ENSG00000197915; -.
DR eggNOG; ENOG502QQH0; Eukaryota.
DR GeneTree; ENSGT00940000154467; -.
DR HOGENOM; CLU_226653_0_0_1; -.
DR InParanoid; Q86YZ3; -.
DR OMA; YGQHESA; -.
DR OrthoDB; 30610at2759; -.
DR TreeFam; TF338665; -.
DR PathwayCommons; Q86YZ3; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q86YZ3; -.
DR BioGRID-ORCS; 388697; 2 hits in 1063 CRISPR screens.
DR GenomeRNAi; 388697; -.
DR Pharos; Q86YZ3; Tbio.
DR PRO; PR:Q86YZ3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q86YZ3; protein.
DR Bgee; ENSG00000197915; Expressed in sural nerve and 79 other tissues.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0001533; C:cornified envelope; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0036457; C:keratohyalin granule; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0043163; P:cell envelope organization; IDA:UniProtKB.
DR GO; GO:0061436; P:establishment of skin barrier; IEP:UniProtKB.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR CDD; cd00213; S-100; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR033201; HRNR.
DR InterPro; IPR034325; S-100_dom.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR22571:SF25; PTHR22571:SF25; 7.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW Calcium; Developmental protein; Keratinization; Metal-binding; Methylation;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..2850
FT /note="Hornerin"
FT /id="PRO_0000144038"
FT DOMAIN 13..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 49..84
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 97..187
FT /note="1"
FT REPEAT 188..278
FT /note="2"
FT REPEAT 279..369
FT /note="3"
FT REPEAT 370..460
FT /note="4"
FT REPEAT 474..566
FT /note="5"
FT REPEAT 593..683
FT /note="6"
FT REPEAT 685..747
FT /note="7"
FT REPEAT 748..836
FT /note="8"
FT REPEAT 839..875
FT /note="9"
FT REPEAT 876..965
FT /note="10"
FT REPEAT 966..1004
FT /note="11"
FT REPEAT 1007..1097
FT /note="12"
FT REPEAT 1098..1188
FT /note="13"
FT REPEAT 1215..1305
FT /note="14"
FT REPEAT 1332..1422
FT /note="15"
FT REPEAT 1423..1474
FT /note="16"
FT REPEAT 1477..1567
FT /note="17"
FT REPEAT 1568..1658
FT /note="18"
FT REPEAT 1685..1775
FT /note="19"
FT REPEAT 1802..1892
FT /note="20"
FT REPEAT 1893..1944
FT /note="21"
FT REPEAT 1947..2037
FT /note="22"
FT REPEAT 2038..2128
FT /note="23"
FT REPEAT 2155..2245
FT /note="24"
FT REPEAT 2272..2362
FT /note="25"
FT REPEAT 2363..2414
FT /note="26"
FT REPEAT 2417..2507
FT /note="27"
FT REPEAT 2508..2598
FT /note="28"
FT REPEAT 2625..2715
FT /note="29"
FT REPEAT 2716..2806
FT /note="30"
FT REGION 1..81
FT /note="S-100-like"
FT REGION 100..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..2817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..2100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2107..2817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 993
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1008
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1205
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHD8"
FT MOD_RES 1463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1712
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1829
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1831
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1933
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1948
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 85
FT /note="R -> H (in dbSNP:rs11204937)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_048494"
FT VARIANT 122
FT /note="R -> W (in dbSNP:rs57277761)"
FT /id="VAR_061053"
FT VARIANT 167
FT /note="G -> D (in dbSNP:rs12741518)"
FT /id="VAR_048495"
FT VARIANT 273
FT /note="H -> Q (in dbSNP:rs7545406)"
FT /id="VAR_059174"
FT VARIANT 376
FT /note="Q -> R (in dbSNP:rs6587649)"
FT /id="VAR_061054"
FT VARIANT 427
FT /note="G -> D (in dbSNP:rs6666097)"
FT /id="VAR_061055"
FT VARIANT 473
FT /note="E -> G (in dbSNP:rs6587648)"
FT /id="VAR_048496"
FT VARIANT 492
FT /note="G -> R (in dbSNP:rs6587647)"
FT /id="VAR_048497"
FT VARIANT 517
FT /note="Y -> C (in dbSNP:rs41266134)"
FT /id="VAR_061056"
FT VARIANT 664
FT /note="R -> Q (in dbSNP:rs7520249)"
FT /id="VAR_048498"
FT VARIANT 799
FT /note="S -> T (in dbSNP:rs6662450)"
FT /id="VAR_048499"
FT VARIANT 2435
FT /note="S -> G (in dbSNP:rs78949172)"
FT /id="VAR_059175"
FT VARIANT 2461
FT /note="G -> S (in dbSNP:rs6659183)"
FT /id="VAR_059176"
FT CONFLICT 271
FT /note="E -> D (in Ref. 2; AAR91619)"
FT /evidence="ECO:0000305"
FT CONFLICT 2382
FT /note="R -> Q (in Ref. 1; BAC57496)"
FT /evidence="ECO:0000305"
FT CONFLICT 2539
FT /note="G -> S (in Ref. 1; BAC57496)"
FT /evidence="ECO:0000305"
FT CONFLICT 2688
FT /note="L -> S (in Ref. 1; BAC57496)"
FT /evidence="ECO:0000305"
FT CONFLICT 2837
FT /note="P -> T (in Ref. 2; AAR91619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2850 AA; 282390 MW; F25D8028C5AB6701 CRC64;
MPKLLQGVIT VIDVFYQYAT QHGEYDTLNK AELKELLENE FHQILKNPND PDTVDIILQS
LDRDHNKKVD FTEYLLMIFK LVQARNKIIG KDYCQVSGSK LRDDTHQHQE EQEETEKEEN
KRQESSFSHS SWSAGENDSY SRNVRGSLKP GTESISRRLS FQRDFSGQHN SYSGQSSSYG
EQNSDSHQSS GRGQCGSGSG QSPNYGQHGS GSGQSSSNDT HGSGSGQSSG FSQHKSSSGQ
SSGYSQHGSG SGHSSGYGQH GSRSGQSSRG ERHRSSSGSS SSYGQHGSGS RQSLGHGRQG
SGSRQSPSHV RHGSGSGHSS SHGQHGSGSS YSYSRGHYES GSGQTSGFGQ HESGSGQSSG
YSKHGSGSGH SSSQGQHGST SGQASSSGQH GSSSRQSSSY GQHESASRHS SGRGQHSSGS
GQSPGHGQRG SGSGQSPSSG QHGTGFGRSS SSGPYVSGSG YSSGFGHHES SSEHSSGYTQ
HGSGSGHSSG HGQHGSRSGQ SSRGERQGSS AGSSSSYGQH GSGSRQSLGH SRHGSGSGQS
PSPSRGRHES GSRQSSSYGP HGYGSGRSSS RGPYESGSGH SSGLGHQESR SGQSSGYGQH
GSSSGHSSTH GQHGSTSGQS SSCGQHGATS GQSSSHGQHG SGSSQSSRYG QQGSGSGQSP
SRGRHGSDFG HSSSYGQHGS GSGWSSSNGP HGSVSGQSSG FGHKSGSGQS SGYSQHGSGS
SHSSGYRKHG SRSGQSSRSE QHGSSSGLSS SYGQHGSGSH QSSGHGRQGS GSGHSPSRVR
HGSSSGHSSS HGQHGSGTSC SSSCGHYESG SGQASGFGQH ESGSGQGYSQ HGSASGHFSS
QGRHGSTSGQ SSSSGQHDSS SGQSSSYGQH ESASHHASGR GRHGSGSGQS PGHGQRGSGS
GQSPSYGRHG SGSGRSSSSG RHGSGSGQSS GFGHKSSSGQ SSGYTQHGSG SGHSSSYEQH
GSRSGQSSRS EQHGSSSGSS SSYGQHGSGS RQSLGHGQHG SGSGQSPSPS RGRHGSGSGQ
SSSYGPYRSG SGWSSSRGPY ESGSGHSSGL GHRESRSGQS SGYGQHGSSS GHSSTHGQHG
STSGQSSSCG QHGASSGQSS SHGQHGSGSS QSSGYGRQGS GSGQSPGHGQ RGSGSRQSPS
YGRHGSGSGR SSSSGQHGSG LGESSGFGHH ESSSGQSSSY SQHGSGSGHS SGYGQHGSRS
GQSSRGERHG SSSGSSSHYG QHGSGSRQSS GHGRQGSGSG HSPSRGRHGS GLGHSSSHGQ
HGSGSGRSSS RGPYESRSGH SSVFGQHESG SGHSSAYSQH GSGSGHFCSQ GQHGSTSGQS
STFDQEGSST GQSSSYGHRG SGSSQSSGYG RHGAGSGQSP SRGRHGSGSG HSSSYGQHGS
GSGWSSSSGR HGSGSGQSSG FGHHESSSWQ SSGCTQHGSG SGHSSSYEQH GSRSGQSSRG
ERHGSSSGSS SSYGQHGSGS RQSLGHGQHG SGSGQSPSPS RGRHGSGSGQ SSSYSPYGSG
SGWSSSRGPY ESGSSHSSGL GHRESRSGQS SGYGQHGSSS GHSSTHGQHG STSGQSSSCG
QHGASSGQSS SHGQHGSGSS QSSGYGRQGS GSGQSPGHGQ RGSGSRQSPS YGRHGSGSGR
SSSSGQHGSG LGESSGFGHH ESSSGQSSSY SQHGSGSGHS SGYGQHGSRS GQSSRGERHG
SSSRSSSRYG QHGSGSRQSS GHGRQGSGSG QSPSRGRHGS GLGHSSSHGQ HGSGSGRSSS
RGPYESRSGH SSVFGQHESG SGHSSAYSQH GSGSGHFCSQ GQHGSTSGQS STFDQEGSST
GQSSSHGQHG SGSSQSSSYG QQGSGSGQSP SRGRHGSGSG HSSSYGQHGS GSGWSSSSGR
HGSGSGQSSG FGHHESSSWQ SSGYTQHGSG SGHSSSYEQH GSRSGQSSRG EQHGSSSGSS
SSYGQHGSGS RQSLGHGQHG SGSGQSPSPS RGRHGSGSGQ SSSYGPYGSG SGWSSSRGPY
ESGSGHSSGL GHRESRSGQS SGYGQHGSSS GHSSTHGQHG SASGQSSSCG QHGASSGQSS
SHGQHGSGSS QSSGYGRQGS GSGQSPGHGQ RGSGSRQSPS YGRHGSGSGR SSSSGQHGPG
LGESSGFGHH ESSSGQSSSY SQHGSGSGHS SGYGQHGSRS GQSSRGERHG SSSGSSSRYG
QHGSGSRQSS GHGRQGSGSG HSPSRGRHGS GSGHSSSHGQ HGSGSGRSSS RGPYESRSGH
SSVFGQHESG SGHSSAYSQH GSGSGHFCSQ GQHGSTSGQS STFDQEGSST GQSSSHGQHG
SGSSQSSSYG QQGSGSGQSP SRGRHGSGSG HSSSYGQHGS GSGWSSSSGR HGSGSGQSSG
FGHHESSSWQ SSGYTQHGSG SGHSSSYEQH GSRSGQSSRG ERHGSSSGSS SSYGQHGSGS
RQSLGHGQHG SGSGQSPSPS RGRHGSGSGQ SSSYSPYGSG SGWSSSRGPY ESGSGHSSGL
GHRESRSGQS SGYGQHGSSS GHSSTHGQHG STSGQSSSCG QHGASSGQSS SHGQHGSGSS
QSSGYGRQGS GSGQSPGHGQ RGSGSRQSPS YGRHGSGSGR SSSSGQHGSG LGESSGFGHH
ESSSGQSSSY SQHGSGSGHS SGYGQHGSRS GQSSRGERHG SSSGSSSHYG QHGSGSRQSS
GHGRQGSGSG QSPSRGRHGS GLGHSSSHGQ HGSGSGRSSS RGPYESRLGH SSVFGQHESG
SGHSSAYSQH GSGSGHFCSQ GQHGSTSGQS STFDQEGSST GQSSSYGHRG SGSSQSSGYG
RHGAGSGQSL SHGRHGSGSG QSSSYGQHGS GSGQSSGYSQ HGSGSGQDGY SYCKGGSNHD
GGSSGSYFLS FPSSTSPYEY VQEQRCYFYQ
