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 02-OCT-2024, entry version 177. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7UAI; EM; 2.80 A; A/H=1-382. DR PDBsum; 6SAZ; -. DR PDBsum; 7UAI; -. DR AlphaFoldDB; Q9UGM5; -. DR EMDB; EMD-26426; -. 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 GlyCosmos; Q9UGM5; 9 sites, 19 glycans. 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; 9606-ENSP00000265029; -. DR PeptideAtlas; Q9UGM5; -. DR ProteomicsDB; 20217; -. DR ProteomicsDB; 84243; -. [Q9UGM5-1] DR Antibodypedia; 33852; 313 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 AGR; HGNC:3658; -. 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; NCQFAHR; -. DR OrthoDB; 5351668at2759; -. DR PhylomeDB; Q9UGM5; -. DR TreeFam; TF333729; -. DR PathwayCommons; Q9UGM5; -. DR SignaLink; Q9UGM5; -. DR BioGRID-ORCS; 26998; 16 hits in 1138 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 72 other cell types or tissues. DR ExpressionAtlas; Q9UGM5; baseline and differential. 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: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 Gene3D; 3.10.450.10; -; 2. DR InterPro; IPR000010; Cystatin_dom. DR InterPro; IPR025764; Cystatin_Fetuin_B. DR InterPro; IPR046350; Cystatin_sf. DR InterPro; IPR050735; Kininogen_Fetuin_HRG. DR InterPro; IPR001363; Prot_inh_fetuin_CS. DR PANTHER; PTHR13814; FETUIN; 1. DR PANTHER; PTHR13814:SF10; FETUIN-B; 1. DR Pfam; PF00031; Cystatin; 2. DR SMART; SM00043; CY; 2. DR SUPFAM; SSF54403; Cystatin/monellin; 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; Proteomics identification; KW Reference proteome; Repeat; Secreted; 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 //