CTSRE_MOUSE
ID CTSRE_MOUSE Reviewed; 985 AA.
AC P0DP43;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Cation channel sperm-associated auxiliary subunit epsilon {ECO:0000250|UniProtKB:Q5SY80};
DE Short=CatSper-epsilon {ECO:0000303|PubMed:28226241};
DE Short=CatSperepsilon {ECO:0000303|PubMed:28226241};
DE AltName: Full=C1orf101-like protein {ECO:0000303|PubMed:28226241};
DE Flags: Precursor;
GN Name=Catspere {ECO:0000303|PubMed:28226241};
GN Synonyms=Catspere1 {ECO:0000312|MGI:MGI:3647531},
GN Gm7068 {ECO:0000312|MGI:MGI:3647531};
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 [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 [2]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
RP CATSPER COMPLEX, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28226241; DOI=10.7554/elife.23082;
RA Chung J.J., Miki K., Kim D., Shim S.H., Shi H.F., Hwang J.Y., Cai X.,
RA Iseri Y., Zhuang X., Clapham D.E.;
RT "CatSperzeta regulates the structural continuity of sperm Ca(2+) signaling
RT domains and is required for normal fertility.";
RL Elife 6:0-0(2017).
RN [3]
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 [4]
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-91; ASN-143; ASN-292;
RP ASN-502; ASN-565; ASN-749; ASN-830; ASN-888 AND ASN-920.
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:28226241,
CC PubMed:34225353). Sperm cell hyperactivation is needed for sperm
CC motility which is essential late in the preparation of sperm for
CC fertilization (PubMed:28226241). {ECO:0000269|PubMed:28226241,
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:28226241, 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:34998468). {ECO:0000250|UniProtKB:Q91ZR5,
CC ECO:0000269|PubMed:28226241, ECO:0000269|PubMed:34225353,
CC ECO:0000269|PubMed:34998468}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000269|PubMed:28226241}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Specifically located in the principal piece of
CC sperm tail. {ECO:0000269|PubMed:28226241}.
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:28226241}.
CC -!- SIMILARITY: Belongs to the CATSPERD family. {ECO:0000305}.
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DR EMBL; AC157787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC163217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006497146.1; XM_006497083.2.
DR PDB; 7EEB; EM; 2.90 A; H=1-985.
DR PDBsum; 7EEB; -.
DR AlphaFoldDB; P0DP43; -.
DR SMR; P0DP43; -.
DR CORUM; P0DP43; -.
DR GlyGen; P0DP43; 2 sites.
DR PhosphoSitePlus; P0DP43; -.
DR PRIDE; P0DP43; -.
DR ProteomicsDB; 285352; -.
DR MGI; MGI:3647531; Catspere1.
DR OrthoDB; 213907at2759; -.
DR ChiTaRS; Gm7068; mouse.
DR PRO; PR:P0DP43; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P0DP43; protein.
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; IBA:GO_Central.
DR GO; GO:0048240; P:sperm capacitation; IBA:GO_Central.
DR InterPro; IPR028751; CATSPERD/E.
DR PANTHER; PTHR33722; PTHR33722; 1.
DR Pfam; PF15020; CATSPERD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cilium; Disulfide bond;
KW Flagellum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..985
FT /note="Cation channel sperm-associated auxiliary subunit
FT epsilon"
FT /evidence="ECO:0000255"
FT /id="PRO_0000440635"
FT TOPO_DOM 36..937
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 938..958
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 959..985
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 830
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 888
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 915
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 920
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT DISULFID 87..101
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 130..235
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 275..365
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 439..442
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 617..724
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 737..919
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 753..786
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 838..869
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 128..140
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 288..297
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 347..350
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 367..372
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 397..402
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 403..409
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 418..425
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 431..438
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 444..455
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 456..459
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 496..500
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 501..504
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 518..521
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 527..532
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 534..542
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 547..551
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 569..574
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 580..585
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 591..599
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 602..613
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 620..624
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 629..633
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 639..648
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 655..661
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 666..676
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 679..689
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 700..706
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 709..719
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 730..736
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 742..745
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 750..753
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 758..762
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 764..766
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 775..779
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 781..784
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 800..803
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 805..811
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 816..822
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 828..832
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 833..836
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 845..851
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 857..860
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 863..865
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 869..871
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 872..875
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 899..901
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 904..911
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 922..928
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 938..966
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 967..969
FT /evidence="ECO:0007829|PDB:7EEB"
SQ SEQUENCE 985 AA; 113803 MW; 2752FB5563DBD80B CRC64;
MPSAGQRKPG SLLALQALQK WLLRGGVGAM LARQVVAALL LWLSCCVSAL WRYYINSQDY
SIFSTRSSIK LEYEGNSFVS WKIPESCKVE NTTSPKTTLH CKRAGIHTIK PIAGNQEVER
HLTVDNSYIC YLWYFTVVDV YYNLSQIVTI WVYDPESAST EELIWTAKKP SLSSRVLTKQ
MNTLGQRPFI FTVEKRLTYH PGPLTSEGTW VIHLPMSSDD IAKVIRGNKV AFQDCFIANL
YFMLTYPMTI ISEPPGYEPL TVPPGSPLML SWDTCISTFA LLATDQETFQ TNDSFQTWTR
VRAPPGILSD AQRHSLRDVI IFDQGTLFLV DGTVYLRTED EFTKLDESRG ISETGILGFS
KRRWCQIRYL YKLASKKSIL IAWSKTTVYA GYATFRFVTL TDTAKLKDFL KLPQTDTLEV
MSVEYLWHPL EAAVLLSHCS VCTTNTRNIR IVIYSAIFQT WTLQDFELQL PKEAILEFRF
LYSAMPDIIM WDQHHVYYSY KNFTVVGTIS TPSGETNLSS LSQGSKIHQV LTDRIGNVVV
KMENNVMFYI KADITEAVIL HTWVNTTAKT VVLFDKSFEV CILYYNENLD EKYQLQTQPY
PLILELQSIN KDLGDWCPYL AFQHNIHSQF YHMDKGESLT IWSQIVYPEN RGLYIVVEHY
GSSVMTWTQN LEYEIASGFC TKTMITRFFQ TTNYELVDNY YQLQKENTGL MLLQFRPSEF
SRTCLTAKPV FEIDVGCDSS KYIMVRGFNK SRCQRRDFSY VIDKELLRES LSDNLKVRYD
VAKYGCPLTL ELGQMFQPIV ELYDENGFIK IVDANFILWE IHGRNDYTFN STMEQNGCIN
EAQTWDSMIE ENPDIPLDDV WGPQNYRPCF SYAIGKPGDL GQPYEILNYS NKNHIKWPMT
YAGMYVYRLK ILDPNYSFCN LTTIFAIESL GMIPRSSVYL VAALIFVLML TFISILVLSY
FWYLKIYRQF IIEPLHKRPA KQKKN
