FBCD1_HUMAN
ID FBCD1_HUMAN Reviewed; 461 AA.
AC Q8N539; A3KFK0; Q6UXK6; Q96SJ7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Fibrinogen C domain-containing protein 1;
GN Name=FIBCD1; ORFNames=UNQ701/PRO1346;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19710473; DOI=10.4049/jimmunol.0901526;
RA Schlosser A., Thomsen T., Moeller J.B., Nielsen O., Tornoee I.,
RA Mollenhauer J., Moestrup S.K., Holmskov U.;
RT "Characterization of FIBCD1 as an acetyl group-binding receptor that binds
RT chitin.";
RL J. Immunol. 183:3800-3809(2009).
RN [6]
RP FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF
RP ASP-393; ASP-395; TYR-405; HIS-415; TYR-431; ALA-432 AND TRP-443.
RX PubMed=19892701; DOI=10.1074/jbc.m109.061523;
RA Thomsen T., Moeller J.B., Schlosser A., Sorensen G.L., Moestrup S.K.,
RA Palaniyar N., Wallis R., Mollenhauer J., Holmskov U.;
RT "The recognition unit of FIBCD1 organizes into a noncovalently linked
RT tetrameric structure and uses a hydrophobic funnel (S1) for acetyl group
RT recognition.";
RL J. Biol. Chem. 285:1229-1238(2010).
CC -!- FUNCTION: Acetyl group-binding receptor which shows a high-affinity and
CC calcium-dependent binding to acetylated structures such as chitin, some
CC N-acetylated carbohydrates, and amino acids, but not to their non-
CC acetylated counterparts. Can facilitate the endocytosis of acetylated
CC components. {ECO:0000269|PubMed:19710473, ECO:0000269|PubMed:19892701}.
CC -!- SUBUNIT: Homotetramer; disulfide-linked. {ECO:0000269|PubMed:19710473,
CC ECO:0000269|PubMed:19892701}.
CC -!- INTERACTION:
CC Q8N539; P21145: MAL; NbExp=6; IntAct=EBI-10200808, EBI-3932027;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N539-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N539-2; Sequence=VSP_026618, VSP_026619, VSP_026620;
CC -!- TISSUE SPECIFICITY: Expressed in the small and large intestinal
CC epithelial cells with a highly polarized localization to the apical
CC surface corresponding to the brush border and in the ducts of the
CC salivary gland. {ECO:0000269|PubMed:19710473}.
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DR EMBL; AY358311; AAQ88678.1; -; mRNA.
DR EMBL; AK027716; BAB55319.1; -; mRNA.
DR EMBL; AL161733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032953; AAH32953.1; -; mRNA.
DR CCDS; CCDS6937.1; -. [Q8N539-1]
DR RefSeq; NP_001138578.1; NM_001145106.1. [Q8N539-1]
DR RefSeq; NP_116232.3; NM_032843.4. [Q8N539-1]
DR PDB; 4M7F; X-ray; 2.10 A; A/B=236-461.
DR PDB; 4M7H; X-ray; 2.00 A; A/B=236-461.
DR PDB; 6ZQR; X-ray; 1.93 A; A/B=236-461.
DR PDB; 6ZQX; X-ray; 1.84 A; A/B=236-461.
DR PDB; 6ZQY; X-ray; 1.85 A; A/B=236-461.
DR PDB; 6ZR0; X-ray; 1.94 A; A/B=236-461.
DR PDB; 6ZR3; X-ray; 1.97 A; A/B=236-461.
DR PDB; 6ZR4; X-ray; 2.00 A; A/B=236-461.
DR PDBsum; 4M7F; -.
DR PDBsum; 4M7H; -.
DR PDBsum; 6ZQR; -.
DR PDBsum; 6ZQX; -.
DR PDBsum; 6ZQY; -.
DR PDBsum; 6ZR0; -.
DR PDBsum; 6ZR3; -.
DR PDBsum; 6ZR4; -.
DR AlphaFoldDB; Q8N539; -.
DR SMR; Q8N539; -.
DR BioGRID; 124363; 15.
DR IntAct; Q8N539; 1.
DR STRING; 9606.ENSP00000361413; -.
DR ChEMBL; CHEMBL4523397; -.
DR UniLectin; Q8N539; -.
DR GlyGen; Q8N539; 1 site.
DR iPTMnet; Q8N539; -.
DR PhosphoSitePlus; Q8N539; -.
DR BioMuta; FIBCD1; -.
DR DMDM; 152032456; -.
DR MassIVE; Q8N539; -.
DR PaxDb; Q8N539; -.
DR PeptideAtlas; Q8N539; -.
DR PRIDE; Q8N539; -.
DR ProteomicsDB; 71998; -. [Q8N539-1]
DR Antibodypedia; 31542; 80 antibodies from 17 providers.
DR DNASU; 84929; -.
DR Ensembl; ENST00000372338.9; ENSP00000361413.4; ENSG00000130720.13. [Q8N539-1]
DR Ensembl; ENST00000448616.5; ENSP00000414501.1; ENSG00000130720.13. [Q8N539-1]
DR GeneID; 84929; -.
DR KEGG; hsa:84929; -.
DR MANE-Select; ENST00000372338.9; ENSP00000361413.4; NM_032843.5; NP_116232.3.
DR UCSC; uc004bzz.4; human. [Q8N539-1]
DR CTD; 84929; -.
DR DisGeNET; 84929; -.
DR GeneCards; FIBCD1; -.
DR HGNC; HGNC:25922; FIBCD1.
DR HPA; ENSG00000130720; Group enriched (adrenal gland, brain, parathyroid gland, testis).
DR MIM; 613357; gene.
DR neXtProt; NX_Q8N539; -.
DR OpenTargets; ENSG00000130720; -.
DR PharmGKB; PA134891641; -.
DR VEuPathDB; HostDB:ENSG00000130720; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000155976; -.
DR HOGENOM; CLU_038628_5_1_1; -.
DR InParanoid; Q8N539; -.
DR OMA; PQRMSCG; -.
DR OrthoDB; 523014at2759; -.
DR PhylomeDB; Q8N539; -.
DR TreeFam; TF351983; -.
DR PathwayCommons; Q8N539; -.
DR SignaLink; Q8N539; -.
DR BioGRID-ORCS; 84929; 35 hits in 1066 CRISPR screens.
DR ChiTaRS; FIBCD1; human.
DR GenomeRNAi; 84929; -.
DR Pharos; Q8N539; Tbio.
DR PRO; PR:Q8N539; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8N539; protein.
DR Bgee; ENSG00000130720; Expressed in right adrenal gland cortex and 142 other tissues.
DR ExpressionAtlas; Q8N539; baseline and differential.
DR Genevisible; Q8N539; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Chitin-binding;
KW Disulfide bond; Glycoprotein; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..461
FT /note="Fibrinogen C domain-containing protein 1"
FT /id="PRO_0000294315"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..461
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 235..458
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 405
FT /note="Implicated in ligand binding"
FT SITE 415
FT /note="Implicated in ligand binding"
FT SITE 431
FT /note="Implicated in ligand binding"
FT SITE 432
FT /note="Implicated in ligand binding"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 244..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 401..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT VAR_SEQ 1..158
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026618"
FT VAR_SEQ 317..357
FT /note="LKRIHALTTQAAYELHVDLEDFENGTAYARYGSFGVGLFSV -> PLDRCTL
FT SLALLVPVAPSPTPPHSFVNVLHPPVPGGPTLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026619"
FT VAR_SEQ 358..461
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026620"
FT MUTAGEN 393
FT /note="D->N: Complete loss of binding to acetylated bovine
FT serum albumin and reduced binding to chitin; when
FT associated with A-395."
FT /evidence="ECO:0000269|PubMed:19892701"
FT MUTAGEN 395
FT /note="D->A: Complete loss of binding to acetylated bovine
FT serum albumin and reduced binding to chitin; when
FT associated with N-395."
FT /evidence="ECO:0000269|PubMed:19892701"
FT MUTAGEN 405
FT /note="Y->S: Significantly reduced binding to acetylated
FT bovine serum albumin and loss of binding to chitin; when
FT associated with S-431."
FT /evidence="ECO:0000269|PubMed:19892701"
FT MUTAGEN 415
FT /note="H->G: Complete loss of binding to acetylated bovine
FT serum albumin and chitin."
FT /evidence="ECO:0000269|PubMed:19892701"
FT MUTAGEN 431
FT /note="Y->S: Significantly reduced binding to acetylated
FT bovine serum albumin and loss of binding to chitin; when
FT associated with S-405."
FT /evidence="ECO:0000269|PubMed:19892701"
FT MUTAGEN 432
FT /note="A->V: Complete loss of binding to acetylated bovine
FT serum albumin and chitin."
FT /evidence="ECO:0000269|PubMed:19892701"
FT MUTAGEN 443
FT /note="W->S: Slight reduction in binding to acetylated
FT bovine serum albumin and no effect on binding to chitin."
FT /evidence="ECO:0000269|PubMed:19892701"
FT CONFLICT 79
FT /note="L -> V (in Ref. 4; AAH32953)"
FT /evidence="ECO:0000305"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:6ZQX"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:6ZQX"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:6ZQX"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:6ZQX"
FT STRAND 282..291
FT /evidence="ECO:0007829|PDB:6ZQX"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:6ZQX"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:6ZQX"
FT HELIX 317..324
FT /evidence="ECO:0007829|PDB:6ZQX"
FT STRAND 329..336
FT /evidence="ECO:0007829|PDB:6ZQX"
FT STRAND 342..353
FT /evidence="ECO:0007829|PDB:6ZQX"
FT TURN 359..363
FT /evidence="ECO:0007829|PDB:6ZQX"
FT STRAND 366..375
FT /evidence="ECO:0007829|PDB:6ZQX"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:6ZQX"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:6ZQX"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:6ZQX"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:6ZQX"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:6ZQX"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:6ZQX"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:6ZQX"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:6ZQX"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:6ZQX"
FT STRAND 448..456
FT /evidence="ECO:0007829|PDB:6ZQX"
SQ SEQUENCE 461 AA; 50744 MW; B217DBFD370A3443 CRC64;
MVNDRWKTMG GAAQLEDRPR DKPQRPSCGY VLCTVLLALA VLLAVAVTGA VLFLNHAHAP
GTAPPPVVST GAASANSALV TVERADSSHL SILIDPRCPD LTDSFARLES AQASVLQALT
EHQAQPRLVG DQEQELLDTL ADQLPRLLAR ASELQTECMG LRKGHGTLGQ GLSALQSEQG
RLIQLLSESQ GHMAHLVNSV SDILDALQRD RGLGRPRNKA DLQRAPARGT RPRGCATGSR
PRDCLDVLLS GQQDDGVYSV FPTHYPAGFQ VYCDMRTDGG GWTVFQRRED GSVNFFRGWD
AYRDGFGRLT GEHWLGLKRI HALTTQAAYE LHVDLEDFEN GTAYARYGSF GVGLFSVDPE
EDGYPLTVAD YSGTAGDSLL KHSGMRFTTK DRDSDHSENN CAAFYRGAWW YRNCHTSNLN
GQYLRGAHAS YADGVEWSSW TGWQYSLKFS EMKIRPVRED R
