FETUB_HUMAN
ID FETUB_HUMAN Reviewed; 382 AA.
AC Q9UGM5; B2RCW6; E9PG06; Q1RMZ0; Q5J876; Q6DK58; Q6GRB6; Q9Y6Z0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Fetuin-B;
DE AltName: Full=16G2;
DE AltName: Full=Fetuin-like protein IRL685;
DE AltName: Full=Gugu;
DE Flags: Precursor;
GN Name=FETUB;
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].
RC TISSUE=Fetus;
RX PubMed=10947975; DOI=10.1042/bj3500589;
RA Olivier E., Soury E., Ruminy P., Husson A., Parmentier F., Daveau M.,
RA Salier J.-P.;
RT "Fetuin-B, a second member of the fetuin family in mammals.";
RL Biochem. J. 350:589-597(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=15499407; DOI=10.1139/g04-043;
RA Hsu S.J., Nagase H., Balmain A.;
RT "Identification of fetuin-B as a member of a cystatin-like gene family on
RT mouse chromosome 16 with tumor suppressor activity.";
RL Genome 47:931-946(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Aihara T., Miyoshi Y., Nakamura Y.;
RT "H16G2, a gene specifically expressed in the liver.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tongue;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-37 AND ASN-136.
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 [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=23562279; DOI=10.1016/j.devcel.2013.03.001;
RA Dietzel E., Wessling J., Floehr J., Schafer C., Ensslen S., Denecke B.,
RA Rosing B., Neulen J., Veitinger T., Spehr M., Tropartz T., Tolba R.,
RA Renne T., Egert A., Schorle H., Gottenbusch Y., Hildebrand A.,
RA Yiallouros I., Stocker W., Weiskirchen R., Jahnen-Dechent W.;
RT "Fetuin-B, a liver-derived plasma protein is essential for fertilization.";
RL Dev. Cell 25:106-112(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP 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: Protease inhibitor required for egg fertilization. Required
CC to prevent premature zona pellucida hardening before fertilization,
CC probably by inhibiting the protease activity of ASTL, a protease that
CC mediates the cleavage of ZP2 and triggers zona pellucida hardening (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UGM5; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-13049494, EBI-6942903;
CC Q9UGM5; Q6PI48: DARS2; NbExp=3; IntAct=EBI-13049494, EBI-3917045;
CC Q9UGM5; Q15125: EBP; NbExp=3; IntAct=EBI-13049494, EBI-3915253;
CC Q9UGM5; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-13049494, EBI-781551;
CC Q9UGM5; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-13049494, EBI-18053395;
CC Q9UGM5; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-13049494, EBI-3923617;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UGM5-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q9UGM5-2; Sequence=VSP_047135;
CC -!- TISSUE SPECIFICITY: Liver and testis.
CC -!- DEVELOPMENTAL STAGE: 2-fold increase toward the end of the menstrual
CC cycle. {ECO:0000269|PubMed:23562279}.
CC -!- SIMILARITY: Belongs to the fetuin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00862}.
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DR EMBL; AJ242928; CAB62538.1; -; mRNA.
DR EMBL; AF534529; AAQ10515.1; -; mRNA.
DR EMBL; AY373820; AAR22507.1; -; mRNA.
DR EMBL; AB017551; BAA78341.1; -; mRNA.
DR EMBL; AK315309; BAG37713.1; -; mRNA.
DR EMBL; AC068631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78186.1; -; Genomic_DNA.
DR EMBL; BC069670; AAH69670.1; -; mRNA.
DR EMBL; BC069820; AAH69820.1; -; mRNA.
DR EMBL; BC074734; AAH74734.1; -; mRNA.
DR EMBL; BC114616; AAI14617.1; -; mRNA.
DR CCDS; CCDS3279.1; -. [Q9UGM5-1]
DR CCDS; CCDS82884.1; -. [Q9UGM5-2]
DR RefSeq; NP_001295006.1; NM_001308077.1. [Q9UGM5-2]
DR RefSeq; NP_001295008.1; NM_001308079.1.
DR RefSeq; NP_055190.2; NM_014375.2. [Q9UGM5-1]
DR RefSeq; XP_011510983.1; XM_011512681.2.
DR PDB; 6SAZ; X-ray; 3.00 A; B/D=1-382.
DR PDBsum; 6SAZ; -.
DR AlphaFoldDB; Q9UGM5; -.
DR SMR; Q9UGM5; -.
DR BioGRID; 117944; 9.
DR IntAct; Q9UGM5; 6.
DR STRING; 9606.ENSP00000265029; -.
DR MEROPS; I25.067; -.
DR MEROPS; I25.950; -.
DR GlyConnect; 1234; 15 N-Linked glycans (2 sites).
DR GlyGen; Q9UGM5; 9 sites, 18 N-linked glycans (2 sites), 2 O-linked glycans (5 sites).
DR iPTMnet; Q9UGM5; -.
DR PhosphoSitePlus; Q9UGM5; -.
DR BioMuta; FETUB; -.
DR DMDM; 109940079; -.
DR CPTAC; non-CPTAC-1115; -.
DR CPTAC; non-CPTAC-1116; -.
DR jPOST; Q9UGM5; -.
DR MassIVE; Q9UGM5; -.
DR PaxDb; Q9UGM5; -.
DR PeptideAtlas; Q9UGM5; -.
DR PRIDE; Q9UGM5; -.
DR ProteomicsDB; 20217; -.
DR ProteomicsDB; 84243; -. [Q9UGM5-1]
DR Antibodypedia; 33852; 291 antibodies from 28 providers.
DR DNASU; 26998; -.
DR Ensembl; ENST00000265029.8; ENSP00000265029.3; ENSG00000090512.12. [Q9UGM5-1]
DR Ensembl; ENST00000382136.3; ENSP00000371571.3; ENSG00000090512.12. [Q9UGM5-2]
DR Ensembl; ENST00000450521.5; ENSP00000404288.1; ENSG00000090512.12. [Q9UGM5-1]
DR GeneID; 26998; -.
DR KEGG; hsa:26998; -.
DR MANE-Select; ENST00000265029.8; ENSP00000265029.3; NM_014375.3; NP_055190.2.
DR UCSC; uc003fqn.3; human. [Q9UGM5-1]
DR CTD; 26998; -.
DR DisGeNET; 26998; -.
DR GeneCards; FETUB; -.
DR HGNC; HGNC:3658; FETUB.
DR HPA; ENSG00000090512; Tissue enriched (liver).
DR MIM; 605954; gene.
DR neXtProt; NX_Q9UGM5; -.
DR OpenTargets; ENSG00000090512; -.
DR PharmGKB; PA28099; -.
DR VEuPathDB; HostDB:ENSG00000090512; -.
DR eggNOG; ENOG502S28K; Eukaryota.
DR GeneTree; ENSGT00950000182930; -.
DR HOGENOM; CLU_044085_1_0_1; -.
DR InParanoid; Q9UGM5; -.
DR OMA; HRGFCLG; -.
DR OrthoDB; 1254847at2759; -.
DR PhylomeDB; Q9UGM5; -.
DR TreeFam; TF333729; -.
DR PathwayCommons; Q9UGM5; -.
DR SignaLink; Q9UGM5; -.
DR BioGRID-ORCS; 26998; 13 hits in 1062 CRISPR screens.
DR GeneWiki; Fetuin-B; -.
DR GenomeRNAi; 26998; -.
DR Pharos; Q9UGM5; Tbio.
DR PRO; PR:Q9UGM5; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UGM5; protein.
DR Bgee; ENSG00000090512; Expressed in right lobe of liver and 70 other tissues.
DR ExpressionAtlas; Q9UGM5; baseline and differential.
DR Genevisible; Q9UGM5; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISS:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0007338; P:single fertilization; ISS:UniProtKB.
DR CDD; cd00042; CY; 2.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR025764; Cystatin_Fetuin_B.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR001363; Prot_inh_fetuin_CS.
DR Pfam; PF00031; Cystatin; 2.
DR SMART; SM00043; CY; 2.
DR SUPFAM; SSF54403; SSF54403; 2.
DR PROSITE; PS51530; CYSTATIN_FETUIN_B; 2.
DR PROSITE; PS01254; FETUIN_1; 1.
DR PROSITE; PS01255; FETUIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Fertilization;
KW Glycoprotein; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW Phosphoprotein; Protease inhibitor; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..382
FT /note="Fetuin-B"
FT /id="PRO_0000008899"
FT DOMAIN 25..138
FT /note="Cystatin fetuin-B-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DOMAIN 149..255
FT /note="Cystatin fetuin-B-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT REGION 262..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q58D62"
FT CARBOHYD 292
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q58D62"
FT DISULFID 93..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DISULFID 117..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DISULFID 151..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DISULFID 216..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT DISULFID 237..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00862"
FT VAR_SEQ 76..112
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15499407"
FT /id="VSP_047135"
FT VARIANT 33
FT /note="S -> P (in dbSNP:rs34522046)"
FT /id="VAR_049061"
FT VARIANT 202
FT /note="G -> S (in dbSNP:rs6785067)"
FT /id="VAR_024449"
FT VARIANT 360
FT /note="K -> R (in dbSNP:rs7999)"
FT /id="VAR_049062"
FT CONFLICT 4
FT /note="L -> F (in Ref. 2; AAR22507)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="L -> P (in Ref. 7; AAH74734)"
FT /evidence="ECO:0000305"
FT CONFLICT 18..19
FT /note="AM -> KL (in Ref. 1; CAB62538)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="N -> K (in Ref. 7; AAH74734)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="S -> P (in Ref. 7; AAI14617)"
FT /evidence="ECO:0000305"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:6SAZ"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:6SAZ"
FT STRAND 58..74
FT /evidence="ECO:0007829|PDB:6SAZ"
FT STRAND 78..94
FT /evidence="ECO:0007829|PDB:6SAZ"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6SAZ"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:6SAZ"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:6SAZ"
FT STRAND 113..124
FT /evidence="ECO:0007829|PDB:6SAZ"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:6SAZ"
FT STRAND 129..141
FT /evidence="ECO:0007829|PDB:6SAZ"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:6SAZ"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6SAZ"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6SAZ"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6SAZ"
FT HELIX 165..180
FT /evidence="ECO:0007829|PDB:6SAZ"
FT STRAND 187..198
FT /evidence="ECO:0007829|PDB:6SAZ"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6SAZ"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:6SAZ"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:6SAZ"
FT STRAND 248..256
FT /evidence="ECO:0007829|PDB:6SAZ"
SQ SEQUENCE 382 AA; 42055 MW; C73977793A30AF8A CRC64;
MGLLLPLALC ILVLCCGAMS PPQLALNPSA LLSRGCNDSD VLAVAGFALR DINKDRKDGY
VLRLNRVNDA QEYRRGGLGS LFYLTLDVLE TDCHVLRKKA WQDCGMRIFF ESVYGQCKAI
FYMNNPSRVL YLAAYNCTLR PVSKKKIYMT CPDCPSSIPT DSSNHQVLEA ATESLAKYNN
ENTSKQYSLF KVTRASSQWV VGPSYFVEYL IKESPCTKSQ ASSCSLQSSD SVPVGLCKGS
LTRTHWEKFV SVTCDFFESQ APATGSENSA VNQKPTNLPK VEESQQKNTP PTDSPSKAGP
RGSVQYLPDL DDKNSQEKGP QEAFPVHLDL TTNPQGETLD ISFLFLEPME EKLVVLPFPK
EKARTAECPG PAQNASPLVL PP
