CTSRB_MOUSE
ID CTSRB_MOUSE Reviewed; 1109 AA.
AC A2RTF1; Q8C0R2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Cation channel sperm-associated auxiliary subunit beta {ECO:0000312|MGI:MGI:2443988};
DE Short=CatSper-beta;
GN Name=Catsperb {ECO:0000312|MGI:MGI:2443988};
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], IDENTIFICATION BY MASS SPECTROMETRY,
RP IDENTIFICATION IN A COMPLEX WITH CATSPER1 AND HSPA1B, TISSUE SPECIFICITY,
RP AND FUNCTION.
RC STRAIN=BALB/cJ;
RX PubMed=17478420; DOI=10.1074/jbc.m701083200;
RA Liu J., Xia J., Cho K.-H., Clapham D.E., Ren D.;
RT "CatSperbeta, a novel transmembrane protein in the CatSper channel
RT complex.";
RL J. Biol. Chem. 282:18945-18952(2007).
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].
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 IDENTIFICATION IN A COMPLEX WITH CATSPER1; CATSPERG2 AND HSPA1B.
RX PubMed=19516020; DOI=10.1095/biolreprod.109.077107;
RA Wang H., Liu J., Cho K.-H., Ren D.;
RT "A novel, single, transmembrane protein CATSPERG is associated with
RT CATSPER1 channel protein.";
RL Biol. Reprod. 81:539-544(2009).
RN [5]
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 [6]
RP IDENTIFICATION IN THE CATSPER COMPLEX.
RC STRAIN=C57BL/6J;
RX PubMed=21224844; DOI=10.1038/ncomms1153;
RA Chung J.J., Navarro B., Krapivinsky G., Krapivinsky L., Clapham D.E.;
RT "A novel gene required for male fertility and functional CATSPER channel
RT formation in spermatozoa.";
RL Nat. Commun. 2:153-153(2011).
RN [7]
RP IDENTIFICATION IN THE CATSPER COMPLEX.
RX PubMed=34998468; DOI=10.1016/j.celrep.2021.110226;
RA Hwang J.Y., Wang H., Lu Y., Ikawa M., Chung J.J.;
RT "C2cd6-encoded CatSpertau targets sperm calcium channel to Ca2+ signaling
RT domains in the flagellar membrane.";
RL Cell Rep. 38:110226-110226(2022).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) OF THE CATSPER COMPLEX,
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
RP TRANSMEMBRANE DOMAIN, TOPOLOGY, DISULFIDE BONDS, AND GLYCOSYLATION AT
RP ASN-90; ASN-118; ASN-672; ASN-915; ASN-923 AND ASN-1017.
RX PubMed=34225353; DOI=10.1038/s41586-021-03742-6;
RA Lin S., Ke M., Zhang Y., Yan Z., Wu J.;
RT "Structure of a mammalian sperm cation channel complex.";
RL Nature 595:746-750(2021).
CC -!- FUNCTION: Auxiliary component of the CatSper complex, a complex
CC involved in sperm cell hyperactivation (PubMed:34225353,
CC PubMed:17478420). Sperm cell hyperactivation is needed for sperm
CC motility which is essential late in the preparation of sperm for
CC fertilization (PubMed:17478420). {ECO:0000269|PubMed:17478420,
CC ECO:0000269|PubMed:34225353}.
CC -!- SUBUNIT: Component of the CatSper complex or CatSpermasome composed of
CC the core pore-forming members CATSPER1, CATSPER2, CATSPER3 and CATSPER4
CC as well as auxiliary members CATSPERB, CATSPERG2, CATSPERD, CATSPERE,
CC CATSPERZ, C2CD6/CATSPERT, SLCO6C1, TMEM249, TMEM262 and EFCAB9
CC (PubMed:34225353, PubMed:21224844, PubMed:17478420, PubMed:19516020,
CC PubMed:34998468). HSPA1 may be an additional auxiliary complex member
CC (PubMed:17478420, PubMed:19516020). The core complex members CATSPER1,
CC CATSPER2, CATSPER3 and CATSPER4 form a heterotetrameric channel
CC (PubMed:34225353). The auxiliary CATSPERB, CATSPERG2, CATSPERD and
CC CATSPERE subunits form a pavilion-like structure over the pore which
CC stabilizes the complex through interactions with CATSPER4, CATSPER3,
CC CATSPER1 and CATSPER2 respectively (PubMed:34225353). SLCO6C1 interacts
CC with CATSPERE and TMEM262/CATSPERH interacts with CATSPERB, further
CC stabilizing the complex (PubMed:34225353). C2CD6/CATSPERT interacts at
CC least with CATSPERD and is required for targeting the CatSper complex
CC in the flagellar membrane (PubMed:34998468).
CC {ECO:0000269|PubMed:17478420, ECO:0000269|PubMed:19516020,
CC ECO:0000269|PubMed:21224844, ECO:0000269|PubMed:34225353,
CC ECO:0000269|PubMed:34998468}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000269|PubMed:17478420, ECO:0000269|PubMed:34225353}; Single-pass
CC membrane protein {ECO:0000269|PubMed:34225353}. Note=Predominantly
CC located in the principal piece of the sperm tail.
CC {ECO:0000269|PubMed:17478420, ECO:0000269|PubMed:34225353}.
CC -!- TISSUE SPECIFICITY: Testis-specific. Specifically present in the
CC principal piece of sperm tail (at protein level). Specifically
CC expressed in the seminiferous tubules but not in the interstitial
CC cells. Within the tubules, it is expressed in spermatocytes and
CC spermatids, but not in spermatogonia. {ECO:0000269|PubMed:17478420}.
CC -!- MISCELLANEOUS: CatSperb is absent in sperm from mice lacking CatSper1,
CC suggesting that stable expression of CatSperb protein requires
CC CatSper1. {ECO:0000269|PubMed:17478420}.
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DR EMBL; EF199807; ABO93459.1; -; mRNA.
DR EMBL; AK030010; BAC26731.1; -; mRNA.
DR EMBL; BC132479; AAI32480.1; -; mRNA.
DR CCDS; CCDS26112.1; -.
DR RefSeq; NP_766611.2; NM_173023.2.
DR PDB; 7EEB; EM; 2.90 A; E=1-1109.
DR PDBsum; 7EEB; -.
DR AlphaFoldDB; A2RTF1; -.
DR SMR; A2RTF1; -.
DR BioGRID; 234824; 3.
DR CORUM; A2RTF1; -.
DR STRING; 10090.ENSMUSP00000052089; -.
DR TCDB; 1.A.1.19.3; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; A2RTF1; 5 sites.
DR iPTMnet; A2RTF1; -.
DR PhosphoSitePlus; A2RTF1; -.
DR PaxDb; A2RTF1; -.
DR PRIDE; A2RTF1; -.
DR ProteomicsDB; 279290; -.
DR Antibodypedia; 49510; 43 antibodies from 16 providers.
DR DNASU; 271036; -.
DR Ensembl; ENSMUST00000055156; ENSMUSP00000052089; ENSMUSG00000047014.
DR GeneID; 271036; -.
DR KEGG; mmu:271036; -.
DR UCSC; uc007otl.2; mouse.
DR CTD; 79820; -.
DR MGI; MGI:2443988; Catsperb.
DR VEuPathDB; HostDB:ENSMUSG00000047014; -.
DR eggNOG; ENOG502QZ5S; Eukaryota.
DR GeneTree; ENSGT00390000008198; -.
DR HOGENOM; CLU_012454_0_0_1; -.
DR InParanoid; A2RTF1; -.
DR OMA; KEPFLEW; -.
DR OrthoDB; 846266at2759; -.
DR PhylomeDB; A2RTF1; -.
DR TreeFam; TF328432; -.
DR Reactome; R-MMU-1300642; Sperm Motility And Taxes.
DR BioGRID-ORCS; 271036; 3 hits in 71 CRISPR screens.
DR PRO; PR:A2RTF1; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; A2RTF1; protein.
DR Bgee; ENSMUSG00000047014; Expressed in spermatocyte and 4 other tissues.
DR ExpressionAtlas; A2RTF1; baseline and differential.
DR GO; GO:0036128; C:CatSper complex; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0034702; C:ion channel complex; TAS:MGI.
DR GO; GO:0097228; C:sperm principal piece; IDA:UniProtKB.
DR GO; GO:0048240; P:sperm capacitation; TAS:MGI.
DR InterPro; IPR028748; CATSPERB.
DR PANTHER; PTHR14705; PTHR14705; 1.
DR Pfam; PF15149; CATSPERB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cilium;
KW Developmental protein; Differentiation; Disulfide bond; Flagellum;
KW Glycoprotein; Membrane; Reference proteome; Spermatogenesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1109
FT /note="Cation channel sperm-associated auxiliary subunit
FT beta"
FT /id="PRO_0000295703"
FT TOPO_DOM 1..1055
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 1056..1078
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 1079..1109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 915
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 923
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 1017
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT DISULFID 35..60
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 189..302
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 330..343
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 720..818
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 831..1039
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 913..922
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 924..939
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT CONFLICT 792
FT /note="D -> G (in Ref. 2; BAC26731)"
FT /evidence="ECO:0000305"
FT CONFLICT 1013
FT /note="P -> T (in Ref. 2; BAC26731)"
FT /evidence="ECO:0000305"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 208..226
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 355..363
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 364..367
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 368..375
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 381..389
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 398..403
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 423..434
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 435..438
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 451..456
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 462..467
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 483..487
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 503..507
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 525..529
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 538..554
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 561..567
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 585..593
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 595..598
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 601..611
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 618..620
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 628..632
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 634..636
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 638..643
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 656..661
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 667..673
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 675..685
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 686..688
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 693..695
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 697..699
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 700..703
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 714..717
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 722..725
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 733..735
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 737..740
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 745..756
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 766..770
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 774..783
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 789..797
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 803..810
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 812..814
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 826..830
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 836..839
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 847..852
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 858..860
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 862..866
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 892..894
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 903..906
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 911..913
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 919..921
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 926..930
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 937..939
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 942..946
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 948..954
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 957..961
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 964..967
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 974..978
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 985..988
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 998..1006
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 1017..1020
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 1023..1032
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 1042..1049
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 1060..1085
FT /evidence="ECO:0007829|PDB:7EEB"
SQ SEQUENCE 1109 AA; 126108 MW; 411A5261B70CED5B CRC64;
MESPLIYVML VLLNVFVFSS GVIHNKGKER TYFSCSGEGI LTGLHTIKLF LTMDNLKVRC
FFRNENQSPS KEILGLFTSG GLAPNMIITN STFYGGYYFK LTPFSNRLEW LIDIPRQNIT
VNTDIAAVEQ WMIKITMHEG LNIYDTEGTL LDLVREPILQ WNLGRVLTEM EVRDLYPEVN
DIKVTKSPCA NDVALIGFMM KPSSNGVFIG KTISGFWTYK ECIWHDLTEI IYAELKDEHQ
GLTVIDLVLT NHFLVILTSL GLYVSSDLRY PTTSQIKLSR AEFCGFERVD YIRGNLWYNE
KCFANRESFE VDYVTITFNR NRTLSESSSC FFSKEPFLHW LPCVFSTIKN EKSIPRVITF
LIDQETDSGI YLFNVQDTKE TYVTVAMLKD GKPSPRPKFP SFHFPSTFTL PLGMIFHPRS
HFLYVYGSQI WVSMDGGNTF EMLCNLFSHH VTKTSNSFYT SDIVFIVEDG RILTTKAGLT
TYSELGILKD AIFTLYYDQL GYIHKLTPEN FDAGSKLLGH GNSGSIFGKR PDLGFEAILV
PQYISTNEMY FFAHVPLTMP TNIQWKKRFK TIHLGKTIEF SKTGLANIKN VYMHKTEPVG
FQTSIHTEII VPFGIENSKD SPCLLSDLEI TYSGKLYYTI KLLSKNPLHE LKSTDVEKSV
LIPGYSSFLI MNITDKWTAS ALATMPQAIK SNLKFLTGSW FLYNFGTAGG RKWSISTRQC
NYWIQQDSLD FMSLNLVKYI DVGNTIDFQF KIIPKAMSTF PIPPVSMVVG NPGLVEVKTQ
GVFDLNENYY LDIHVSGRFF QKGSTSIALV LWEGSSKCYA ITLLPTIKSS CSYLRTMHHT
PGRHIPPEDW ISGVHKDSQG FNMIKTLPIN YRPPSHMGIS IPLTDNFYHA DPSKPIPRNQ
FHKSKETGKY KQCANVTSRA MCNCSEHQKF SHAVAFSDCK EKVHRFKFPV TQYPVVLEIF
NERDKISAEP PYLVTMTEVN MRKNWQLKHN EPENVKKMKH YLEPLLKTPV YNPLGLNLTI
QGSELFHFKV SVVPGVSFCE LSEEFQIYVD EVPLPFPGHA LIAVATSVVL GVLIFIAFVF
QLRNIHPLKA LKKSIRGNPG LTSSTTVSS
