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   24-JAN-2024, entry version 174.
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   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; 332 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; 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.
DR   Genevisible; Q9UGM5; HS.
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
//