CTSRD_MOUSE
ID CTSRD_MOUSE Reviewed; 805 AA.
AC E9Q9F6; E7DZL7; E7DZL8; E9Q710; Q1JPR3; Q1LZJ6; Q8C5U5;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Cation channel sperm-associated auxiliary subunit delta {ECO:0000312|MGI:MGI:2147030};
DE Short=CatSper-delta;
DE Short=CatSperdelta;
DE AltName: Full=Transmembrane protein 146;
DE Flags: Precursor;
GN Name=Catsperd {ECO:0000312|MGI:MGI:2147030}; Synonyms=Tmem146;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, IDENTIFICATION IN THE CATSPER COMPLEX, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-805 (ISOFORM 3).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 297-805 (ISOFORMS 1 AND 3).
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 [6]
RP IDENTIFICATION IN THE CATSPER COMPLEX, AND SUBCELLULAR LOCATION.
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 [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) OF THE CATSPER COMPLEX,
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, TRANSMEMBRANE DOMAIN,
RP TOPOLOGY, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-227; ASN-469; ASN-535
RP AND ASN-627.
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). Sperm cell
CC hyperactivation is needed for sperm motility which is essential late in
CC the preparation of sperm for fertilization (PubMed:21224844). Required
CC for CATSPER1 stability before intraflagellar transport and/or
CC incorporation of the CatSper complex channel into the flagellar
CC membrane (PubMed:21224844). {ECO:0000269|PubMed:21224844,
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:34998468). HSPA1 may be an
CC additional auxiliary complex member (By similarity). The core complex
CC members CATSPER1, CATSPER2, CATSPER3 and CATSPER4 form a
CC heterotetrameric channel (PubMed:34225353). The auxiliary CATSPERB,
CC CATSPERG2, CATSPERD and CATSPERE subunits form a pavilion-like
CC structure over the pore which stabilizes the complex through
CC interactions with CATSPER4, CATSPER3, CATSPER1 and CATSPER2
CC respectively (PubMed:34225353). SLCO6C1 interacts with CATSPERE and
CC TMEM262/CATSPERH interacts with CATSPERB, further stabilizing the
CC complex (PubMed:34225353). C2CD6/CATSPERT interacts at least with
CC CATSPERD and is required for targeting the CatSper complex in the
CC flagellar membrane (PubMed:34225353). {ECO:0000250|UniProtKB:Q91ZR5,
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:21224844, ECO:0000269|PubMed:34225353}; Single-pass
CC type I membrane protein {ECO:0000255}. Note=Specifically located in the
CC principal piece of sperm tail. {ECO:0000269|PubMed:21224844,
CC ECO:0000269|PubMed:34225353}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Tmem146-l, l;
CC IsoId=E9Q9F6-1; Sequence=Displayed;
CC Name=2; Synonyms=Tmem146-s, s;
CC IsoId=E9Q9F6-2; Sequence=VSP_042980, VSP_042981;
CC Name=3;
CC IsoId=E9Q9F6-3; Sequence=VSP_042982;
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:21224844}.
CC -!- DEVELOPMENTAL STAGE: Expressed in spermatocytes and spermatids in
CC different stages of spermatogenesis (at protein level).
CC {ECO:0000269|PubMed:21224844}.
CC -!- DISRUPTION PHENOTYPE: Mice are normal but males are sterile. Male
CC sterility is due to defects in sperm cell hyperactivation and decreased
CC stability of Catsper1. {ECO:0000269|PubMed:21224844}.
CC -!- SIMILARITY: Belongs to the CATSPERD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI16634.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC36602.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EDL38183.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HQ441159; ADU32560.1; -; mRNA.
DR EMBL; HQ441160; ADU32561.1; -; mRNA.
DR EMBL; CT010491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT485788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466537; EDL38183.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK077082; BAC36602.1; ALT_INIT; mRNA.
DR EMBL; BC115864; AAI15865.1; -; mRNA.
DR EMBL; BC116633; AAI16634.1; ALT_INIT; mRNA.
DR CCDS; CCDS50153.1; -. [E9Q9F6-1]
DR RefSeq; NP_780559.2; NM_175350.3. [E9Q9F6-1]
DR PDB; 7EEB; EM; 2.90 A; G=1-805.
DR PDBsum; 7EEB; -.
DR AlphaFoldDB; E9Q9F6; -.
DR SMR; E9Q9F6; -.
DR CORUM; E9Q9F6; -.
DR STRING; 10090.ENSMUSP00000108603; -.
DR TCDB; 1.A.1.19.3; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; E9Q9F6; 2 sites.
DR PhosphoSitePlus; E9Q9F6; -.
DR PaxDb; E9Q9F6; -.
DR PRIDE; E9Q9F6; -.
DR ProteomicsDB; 285430; -. [E9Q9F6-1]
DR ProteomicsDB; 285431; -. [E9Q9F6-2]
DR ProteomicsDB; 285432; -. [E9Q9F6-3]
DR Antibodypedia; 11727; 51 antibodies from 16 providers.
DR DNASU; 106757; -.
DR Ensembl; ENSMUST00000112979; ENSMUSP00000108603; ENSMUSG00000040828. [E9Q9F6-1]
DR GeneID; 106757; -.
DR KEGG; mmu:106757; -.
DR UCSC; uc008dcr.2; mouse. [E9Q9F6-3]
DR UCSC; uc008dcs.2; mouse. [E9Q9F6-1]
DR CTD; 257062; -.
DR MGI; MGI:2147030; Catsperd.
DR VEuPathDB; HostDB:ENSMUSG00000040828; -.
DR eggNOG; ENOG502QSPE; Eukaryota.
DR GeneTree; ENSGT00940000162714; -.
DR HOGENOM; CLU_019182_0_0_1; -.
DR InParanoid; E9Q9F6; -.
DR OMA; QDNYSFI; -.
DR OrthoDB; 213907at2759; -.
DR PhylomeDB; E9Q9F6; -.
DR TreeFam; TF337973; -.
DR Reactome; R-MMU-1300642; Sperm Motility And Taxes.
DR BioGRID-ORCS; 106757; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Catsperd; mouse.
DR PRO; PR:E9Q9F6; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; E9Q9F6; protein.
DR Bgee; ENSMUSG00000040828; Expressed in spermatocyte and 53 other tissues.
DR ExpressionAtlas; E9Q9F6; baseline and differential.
DR Genevisible; E9Q9F6; MM.
DR GO; GO:0036128; C:CatSper complex; IDA:UniProtKB.
DR GO; GO:0097228; C:sperm principal piece; IDA:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0048240; P:sperm capacitation; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR InterPro; IPR028751; CATSPERD/E.
DR PANTHER; PTHR33722; PTHR33722; 1.
DR Pfam; PF15020; CATSPERD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection; Cilium;
KW Developmental protein; Differentiation; Disulfide bond; Flagellum;
KW Glycoprotein; Membrane; Reference proteome; Signal; Spermatogenesis;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..805
FT /note="Cation channel sperm-associated auxiliary subunit
FT delta"
FT /id="PRO_0000416884"
FT TOPO_DOM 17..723
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 724..745
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 746..805
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT DISULFID 20..366
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 56..143
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 142..149
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 384..493
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 507..701
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 522..569
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 621..651
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT VAR_SEQ 1..182
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:21224844"
FT /id="VSP_042980"
FT VAR_SEQ 385
FT /note="N -> NVELLESTMINTMFTIDMNSKLKLSALMIPRKGENPTPL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:21224844"
FT /id="VSP_042981"
FT VAR_SEQ 386..423
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_042982"
FT CONFLICT 112
FT /note="G -> V (in Ref. 1; ADU32560)"
FT /evidence="ECO:0000305"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 206..221
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 259..269
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 346..353
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 360..369
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 406..414
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 432..443
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 449..459
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 468..471
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 478..486
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 499..506
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 512..515
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 529..533
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 571..577
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 583..587
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 590..594
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 599..605
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 610..613
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 628..630
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 645..647
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 678..680
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 685..693
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 696..698
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 704..712
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 725..740
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 742..747
FT /evidence="ECO:0007829|PDB:7EEB"
SQ SEQUENCE 805 AA; 91096 MW; B66F82B2D928C08C CRC64;
MLVLMLAAAV ATMVRAHTLC RVHTVRTGKV FKSNIQLQGD PLFYAFPNTF VLKNVCKADI
SVYLGQKVFL TIDNFESSLL PLTVPKSLAV GVPSITSAHF VSGSLVLFVI SGKGYSYDYY
ENTWRKLEGI SEPVSHISGD VCCFKGSFCL ELSNNLFAYL RGGQIPGTNI YFSDNGGFSF
QLMNTDKLSH LTGTLGGIFH LHSMSQVGVL MVENNLGTFH YMEYPLNHSM GIAFSYKNLL
EVIMKPYQRG FMVLWNQKSI LVSSNSGQIV EHVRLIDQKI FTDLDVEHAN INIYSVASNA
YELAFLVAED HLYYGSQSYM GTYVIKLPHQ PLWSTHTSIY FEDIGILQVL TPVADPHFAA
YDFDKCTVNV QSSLMDEKLA LQPCNVELLE STMINTMFTI DMNSKLKLSA LMIPRKGENP
TPLVMVSNPH ALGFKANLNE FGNTFDGNSK YKLDIELKQQ HHWGNSDFNF TASIKRHAIS
SVTVDIADKT LSCVDLKPLS TLISVGCDMT KKIVVQNKIS ACTMGILNPV QLQKNYTYTI
EKEAYDPINH NGEAQDDLIV FYEYKDLGCP RLVYYDKPWK PVVELWKNGI VEEIMNAEYV
ISEINGLVTY SYSLTAATAN CRSQPQNWST FESDIENEEP FLWNRENYVS CHEDNKDNPL
LWPNVEYQVL GGQTNNKIIF GQRNGIYTFH LSVVDPYYSY CNLNTIFSVY VHGALPVTKF
QPLLTILLMV TTTLLTAWLA YAIPKQLRSE KGQRLLGFCY QILQLCLGVC FCTWLRGKLR
QWLRPRRVKD QNRGKVRVAQ KHPET
