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TX101_MOUSE
ID   TX101_MOUSE             Reviewed;         250 AA.
AC   Q9JMI7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Testis-expressed protein 101 {ECO:0000250|UniProtKB:Q9BY14};
DE   AltName: Full=TES101-reactive protein;
DE            Short=TES101RP;
DE   Flags: Precursor;
GN   Name=Tex101 {ECO:0000312|MGI:MGI:1930791};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-44, SUBCELLULAR
RP   LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=11207211; DOI=10.1095/biolreprod64.3.935;
RA   Kurita A., Takizawa T., Takayama T., Totsukawa K., Matsubara S.,
RA   Shibahara H., Orgebin-Crist M.-C., Sendo F., Shinkai Y., Araki Y.;
RT   "Identification, cloning, and initial characterization of a novel mouse
RT   testicular germ cell-specific antigen.";
RL   Biol. Reprod. 64:935-945(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15689535; DOI=10.1095/biolreprod.104.038810;
RA   Takayama T., Mishima T., Mori M., Jin H., Tsukamoto H., Takahashi K.,
RA   Takizawa T., Kinoshita K., Suzuki M., Sato I., Matsubara S., Araki Y.,
RA   Takizawa T.;
RT   "Sexually dimorphic expression of the novel germ cell antigen TEX101 during
RT   mouse gonad development.";
RL   Biol. Reprod. 72:1315-1323(2005).
RN   [5]
RP   SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15917346; DOI=10.1095/biolreprod.105.041533;
RA   Sleight S.B., Miranda P.V., Plaskett N.-W., Maier B., Lysiak J.,
RA   Scrable H., Herr J.C., Visconti P.E.;
RT   "Isolation and proteomic analysis of mouse sperm detergent-resistant
RT   membrane fractions: evidence for dissociation of lipid rafts during
RT   capacitation.";
RL   Biol. Reprod. 73:721-729(2005).
RN   [6]
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP   SHEDDING.
RX   PubMed=16388701; DOI=10.1017/s0967199405003394;
RA   Takayama T., Mishima T., Mori M., Ishikawa T., Takizawa T., Goto T.,
RA   Suzuki M., Araki Y., Matsubara S., Takizawa T.;
RT   "TEX101 is shed from the surface of sperm located in the caput epididymidis
RT   of the mouse.";
RL   Zygote 13:325-333(2005).
RN   [7]
RP   INTERACTION WITH VAMP3, IDENTIFICATION BY MASS SPECTROMETRY, DEVELOPMENTAL
RP   STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=16678124; DOI=10.1016/j.bbrc.2006.04.070;
RA   Tsukamoto H., Yoshitake H., Mori M., Yanagida M., Takamori K., Ogawa H.,
RA   Takizawa T., Araki Y.;
RT   "Testicular proteins associated with the germ cell-marker, TEX101:
RT   involvement of cellubrevin in TEX101-trafficking to the cell surface during
RT   spermatogenesis.";
RL   Biochem. Biophys. Res. Commun. 345:229-238(2006).
RN   [8]
RP   GLYCOSYLATION, AND TOPOLOGY.
RX   PubMed=16822331; DOI=10.1017/s0967199406003753;
RA   Jin H., Yoshitake H., Tsukamoto H., Takahashi M., Mori M., Takizawa T.,
RA   Takamori K., Ogawa H., Kinoshita K., Araki Y.;
RT   "Molecular characterization of a germ-cell-specific antigen, TEX101, from
RT   mouse testis.";
RL   Zygote 14:201-208(2006).
RN   [9]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH LY6K.
RX   PubMed=18503752; DOI=10.1016/j.bbrc.2008.05.088;
RA   Yoshitake H., Tsukamoto H., Maruyama-Fukushima M., Takamori K., Ogawa H.,
RA   Araki Y.;
RT   "TEX101, a germ cell-marker glycoprotein, is associated with lymphocyte
RT   antigen 6 complex locus k within the mouse testis.";
RL   Biochem. Biophys. Res. Commun. 372:277-282(2008).
RN   [10]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX   PubMed=18620756; DOI=10.1016/j.jri.2008.05.001;
RA   Yoshitake H., Shirai Y., Mochizuki Y., Iwanari H., Tsubamoto H., Koyama K.,
RA   Takamori K., Ogawa H., Hasegawa A., Kodama T., Hamakubo T., Araki Y.;
RT   "Molecular diversity of TEX101, a marker glycoprotein for germ cells
RT   monitored with monoclonal antibodies: variety of the molecular
RT   characteristics according to subcellular localization within the mouse
RT   testis.";
RL   J. Reprod. Immunol. 79:1-11(2008).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [12]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH DPEP3.
RX   PubMed=21724266; DOI=10.1016/j.jri.2011.04.010;
RA   Yoshitake H., Yanagida M., Maruyama M., Takamori K., Hasegawa A., Araki Y.;
RT   "Molecular characterization and expression of dipeptidase 3, a testis-
RT   specific membrane-bound dipeptidase: complex formation with TEX101, a germ-
RT   cell-specific antigen in the mouse testis.";
RL   J. Reprod. Immunol. 90:202-213(2011).
RN   [13]
RP   TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, INTERACTION WITH ADAM3 AND ADAM5,
RP   AND FUNCTION.
RX   PubMed=23969891; DOI=10.1093/jmcb/mjt031;
RA   Li W., Guo X.J., Teng F., Hou X.J., Lv Z., Zhou S.Y., Bi Y., Wan H.F.,
RA   Feng C.J., Yuan Y., Zhao X.Y., Wang L., Sha J.H., Zhou Q.;
RT   "Tex101 is essential for male fertility by affecting sperm migration into
RT   the oviduct in mice.";
RL   J. Mol. Cell Biol. 5:345-347(2013).
RN   [14]
RP   TISSUE SPECIFICITY, INTERACTION WITH ADAM3, SHEDDING, AND FUNCTION.
RX   PubMed=23633567; DOI=10.1073/pnas.1222166110;
RA   Fujihara Y., Tokuhiro K., Muro Y., Kondoh G., Araki Y., Ikawa M., Okabe M.;
RT   "Expression of TEX101, regulated by ACE, is essential for the production of
RT   fertile mouse spermatozoa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:8111-8116(2013).
RN   [15]
RP   SHEDDING.
RX   PubMed=24501175; DOI=10.1095/biolreprod.113.112888;
RA   Fujihara Y., Okabe M., Ikawa M.;
RT   "GPI-anchored protein complex, LY6K/TEX101, is required for sperm migration
RT   into the oviduct and male fertility in mice.";
RL   Biol. Reprod. 90:60-60(2014).
RN   [16]
RP   SUBCELLULAR LOCATION.
RX   PubMed=27005865; DOI=10.1038/srep23616;
RA   Endo S., Yoshitake H., Tsukamoto H., Matsuura H., Kato K., Sakuraba M.,
RA   Takamori K., Fujiwara H., Takeda S., Araki Y.;
RT   "TEX101, a glycoprotein essential for sperm fertility, is required for
RT   stable expression of Ly6k on testicular germ cells.";
RL   Sci. Rep. 6:23616-23616(2016).
CC   -!- FUNCTION: Plays a role in fertilization by controlling binding of sperm
CC       to zona pellucida and migration of spermatozoa into the oviduct
CC       probably through molecule adhesion ADAM3 (PubMed:23633567,
CC       PubMed:23969891). May play a role in signal transduction and promote
CC       protein tyrosine phosphorylation (By similarity).
CC       {ECO:0000250|UniProtKB:Q924B5, ECO:0000269|PubMed:23633567,
CC       ECO:0000269|PubMed:23969891}.
CC   -!- SUBUNIT: Interacts with VAMP3 (PubMed:16678124). Interacts with LY6K
CC       (PubMed:18503752). Interacts with DPEP3; co-localized on the cell
CC       surface of spermatocytes, spermatids, and testicular spermatozoa, co-
CC       localized only in cytoplasmic droplets of caput and corpus epididymal
CC       sperm (PubMed:21724266). Interacts with ADAM3; co-localized on sperm
CC       surface (PubMed:23633567, PubMed:23969891). Interacts with ADAM5
CC       (PubMed:23969891). {ECO:0000269|PubMed:16678124,
CC       ECO:0000269|PubMed:18503752, ECO:0000269|PubMed:21724266,
CC       ECO:0000269|PubMed:23633567, ECO:0000269|PubMed:23969891}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11207211,
CC       ECO:0000269|PubMed:16388701, ECO:0000269|PubMed:16678124,
CC       ECO:0000269|PubMed:18503752, ECO:0000269|PubMed:18620756,
CC       ECO:0000269|PubMed:21724266, ECO:0000269|PubMed:27005865}; Lipid-
CC       anchor, GPI-anchor {ECO:0000269|PubMed:16822331}. Membrane raft
CC       {ECO:0000269|PubMed:15917346, ECO:0000269|PubMed:18503752}. Cytoplasmic
CC       vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:27005865}.
CC       Secreted {ECO:0000269|PubMed:18503752, ECO:0000269|PubMed:18620756,
CC       ECO:0000269|PubMed:21724266}. Cytoplasmic vesicle
CC       {ECO:0000269|PubMed:21724266, ECO:0000269|PubMed:27005865}.
CC       Note=Located on plasma membrane of spermatocytes, round and elongated
CC       spermatids, and testicular spermatozoa. {ECO:0000269|PubMed:18620756}.
CC   -!- TISSUE SPECIFICITY: Detected in testis and ovary (PubMed:11207211,
CC       PubMed:15689535, PubMed:15917346, PubMed:16388701, PubMed:23969891).
CC       Expressed in spermatocytes, spermatids and testicular spermatozoa, but
CC       not in spermatogonia or interstitial cells (PubMed:18620756). Expressed
CC       abundantly in testicular germ cells (TGCs) but mostly disappeared from
CC       epididymal spermatozoa (PubMed:23633567). {ECO:0000269|PubMed:11207211,
CC       ECO:0000269|PubMed:15689535, ECO:0000269|PubMed:15917346,
CC       ECO:0000269|PubMed:16388701, ECO:0000269|PubMed:18620756,
CC       ECO:0000269|PubMed:23633567, ECO:0000269|PubMed:23969891}.
CC   -!- DEVELOPMENTAL STAGE: Detected in prospermatogonia in embryos after 14
CC       days of development and until 8 days after birth. Not detectable in
CC       spermatogonia from over 10 day old animals. Highly expressed in
CC       spermatocytes and spermatids from 12-28 day old animals, but not in
CC       spermatogonia. Detected in embryonic ovary after 14 days of development
CC       and in newly born animals. Expression is much reduced in ovary from 4
CC       day old animals, and not detectable thereafter. Not detectable in
CC       oocytes that are surrounded by follicular cells.
CC       {ECO:0000269|PubMed:11207211, ECO:0000269|PubMed:15689535,
CC       ECO:0000269|PubMed:16388701, ECO:0000269|PubMed:16678124}.
CC   -!- PTM: N-glycosylated; by high mannose and/or biantennary complex and/or
CC       certain types of hybrid oligosaccharides; possesses different
CC       oligosaccharides chains according to its subcellular localization in
CC       the testis. {ECO:0000269|PubMed:16822331, ECO:0000269|PubMed:18620756}.
CC   -!- PTM: Sheds from membrane raft by ACE and released from the cell surface
CC       of epididymal sperm while it passes through the caput epididymis
CC       leading to disappearance of TEX101 on spermatozoa; is essential to
CC       produce fertile spermatozoa. {ECO:0000269|PubMed:16388701,
CC       ECO:0000269|PubMed:23633567, ECO:0000269|PubMed:24501175}.
CC   -!- DISRUPTION PHENOTYPE: Knockout Tex101 mice are viable and show no overt
CC       developmental abnormalities. Males are infertile.
CC       {ECO:0000269|PubMed:23969891, ECO:0000269|PubMed:24501175}.
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DR   EMBL; AB022914; BAA90265.1; -; mRNA.
DR   EMBL; BC048475; AAH48475.1; -; mRNA.
DR   EMBL; AK005769; BAB24228.1; -; mRNA.
DR   CCDS; CCDS20959.1; -.
DR   RefSeq; NP_064365.1; NM_019981.2.
DR   PDB; 7BPS; X-ray; 2.35 A; A/B=26-224.
DR   PDBsum; 7BPS; -.
DR   AlphaFoldDB; Q9JMI7; -.
DR   SMR; Q9JMI7; -.
DR   STRING; 10090.ENSMUSP00000077150; -.
DR   GlyGen; Q9JMI7; 4 sites.
DR   PhosphoSitePlus; Q9JMI7; -.
DR   PaxDb; Q9JMI7; -.
DR   PeptideAtlas; Q9JMI7; -.
DR   PRIDE; Q9JMI7; -.
DR   ProteomicsDB; 298439; -.
DR   Antibodypedia; 31041; 40 antibodies from 17 providers.
DR   DNASU; 56746; -.
DR   Ensembl; ENSMUST00000078001; ENSMUSP00000077150; ENSMUSG00000062773.
DR   GeneID; 56746; -.
DR   KEGG; mmu:56746; -.
DR   UCSC; uc009fqf.1; mouse.
DR   CTD; 83639; -.
DR   MGI; MGI:1930791; Tex101.
DR   VEuPathDB; HostDB:ENSMUSG00000062773; -.
DR   eggNOG; ENOG502T90B; Eukaryota.
DR   GeneTree; ENSGT00530000063351; -.
DR   HOGENOM; CLU_077973_0_0_1; -.
DR   InParanoid; Q9JMI7; -.
DR   OMA; QETVLMI; -.
DR   OrthoDB; 1103796at2759; -.
DR   PhylomeDB; Q9JMI7; -.
DR   TreeFam; TF337286; -.
DR   Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   BioGRID-ORCS; 56746; 0 hits in 71 CRISPR screens.
DR   PRO; PR:Q9JMI7; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9JMI7; protein.
DR   Bgee; ENSMUSG00000062773; Expressed in spermatocyte and 26 other tissues.
DR   ExpressionAtlas; Q9JMI7; baseline and differential.
DR   Genevisible; Q9JMI7; MM.
DR   GO; GO:0002080; C:acrosomal membrane; IDA:MGI.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR   GO; GO:0031225; C:anchored component of membrane; ISO:MGI.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0044853; C:plasma membrane raft; IBA:GO_Central.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:UniProtKB.
DR   GO; GO:0009566; P:fertilization; IMP:UniProtKB.
DR   GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR   GO; GO:0002696; P:positive regulation of leukocyte activation; ISO:MGI.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR   GO; GO:1901317; P:regulation of flagellated sperm motility; IMP:UniProtKB.
DR   InterPro; IPR016054; LY6_UPA_recep-like.
DR   Pfam; PF00021; UPAR_LY6; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cytoplasmic vesicle;
KW   Direct protein sequencing; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:11207211"
FT   CHAIN           26..224
FT                   /note="Testis-expressed protein 101"
FT                   /id="PRO_0000247623"
FT   PROPEP          225..250
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000247624"
FT   DOMAIN          141..215
FT                   /note="UPAR/Ly6"
FT   LIPID           224
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   STRAND          31..38
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   HELIX           40..43
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   STRAND          58..67
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   STRAND          73..84
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   STRAND          89..95
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   STRAND          101..109
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   TURN            121..123
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   STRAND          140..142
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   STRAND          144..148
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   STRAND          164..174
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   STRAND          179..189
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   TURN            194..197
FT                   /evidence="ECO:0007829|PDB:7BPS"
FT   STRAND          204..214
FT                   /evidence="ECO:0007829|PDB:7BPS"
SQ   SEQUENCE   250 AA;  26998 MW;  37A1FF7E5C587745 CRC64;
     MGACRIQYVL LIFLLIASRW TLVQNTYCQV SQTLSLEDDP GRTFNWTSKA EQCNPGELCQ
     ETVLLIKADG TRTVVLASKS CVSQGGEAVT FIQYTAPPGL VAISYSNYCN DSLCNNKDSL
     ASVWRVPETT ATSNMSGTRH CPTCVALGSC SSAPSMPCAN GTTQCYQGRL EFSGGGMDAT
     VQVKGCTTTI GCRLMAMIDS VGPMTVKETC SYQSFLQPRK AEIGASQMPT SLWVLELLFP
     LLLLPLTHFP
 
 
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