CTSG2_MOUSE
ID CTSG2_MOUSE Reviewed; 1145 AA.
AC C6KI89;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Cation channel sperm-associated auxiliary subunit gamma 2 {ECO:0000312|MGI:MGI:1923968};
DE Flags: Precursor;
GN Name=Catsperg2 {ECO:0000312|MGI:MGI:1923968}; Synonyms=Catsperg;
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] {ECO:0000305, ECO:0000312|EMBL:ACT09363.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP IDENTIFICATION IN A COMPLEX WITH CATSPER1; CATSPERB AND HSPA1B, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:ACT09363.1};
RC TISSUE=Testis {ECO:0000312|EMBL:ACT09363.1};
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 [2] {ECO:0000305}
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 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 [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-103; ASN-178; ASN-356;
RP ASN-402 AND ASN-672.
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:19516020). Sperm cell hyperactivation is needed for sperm
CC motility which is essential late in the preparation of sperm for
CC fertilization (PubMed:19516020). {ECO:0000269|PubMed:19516020,
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:19516020). HSPA1 may be an
CC additional auxiliary complex member (PubMed:19516020). 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 (Probable). {ECO:0000269|PubMed:19516020,
CC ECO:0000269|PubMed:21224844, ECO:0000269|PubMed:34225353, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Testis-specific. Specifically expressed in the
CC principal piece of the sperm tail (at protein level). Expressed in
CC spermatocytes and spermatids within the seminiferous tubule but not in
CC interstitial cells. {ECO:0000269|PubMed:19516020}.
CC -!- MISCELLANEOUS: Catsperg2 is absent in sperm from mice lacking Catsper1,
CC suggesting that stable expression requires Catsper1.
CC -!- SIMILARITY: Belongs to the CATSPERG family. {ECO:0000305}.
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DR EMBL; GQ225581; ACT09363.1; -; mRNA.
DR EMBL; AC112789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS52173.1; -.
DR RefSeq; NP_083990.2; NM_029714.3.
DR RefSeq; XP_006540475.1; XM_006540412.2.
DR RefSeq; XP_017167870.1; XM_017312381.1.
DR PDB; 7EEB; EM; 2.90 A; F=1-1145.
DR PDBsum; 7EEB; -.
DR AlphaFoldDB; C6KI89; -.
DR SMR; C6KI89; -.
DR BioGRID; 218276; 3.
DR CORUM; C6KI89; -.
DR STRING; 10090.ENSMUSP00000052285; -.
DR TCDB; 1.A.1.19.3; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; C6KI89; 1 site.
DR iPTMnet; C6KI89; -.
DR PhosphoSitePlus; C6KI89; -.
DR PaxDb; C6KI89; -.
DR PRIDE; C6KI89; -.
DR ProteomicsDB; 279289; -.
DR Ensembl; ENSMUST00000061193; ENSMUSP00000052285; ENSMUSG00000049123.
DR Ensembl; ENSMUST00000209126; ENSMUSP00000147099; ENSMUSG00000049123.
DR GeneID; 76718; -.
DR KEGG; mmu:76718; -.
DR UCSC; uc012fhg.1; mouse.
DR CTD; 76718; -.
DR MGI; MGI:1923968; Catsperg2.
DR VEuPathDB; HostDB:ENSMUSG00000049123; -.
DR eggNOG; ENOG502QWAR; Eukaryota.
DR GeneTree; ENSGT00390000014139; -.
DR HOGENOM; CLU_010744_0_0_1; -.
DR InParanoid; C6KI89; -.
DR OMA; RWWKNRK; -.
DR OrthoDB; 110808at2759; -.
DR PhylomeDB; C6KI89; -.
DR TreeFam; TF337337; -.
DR Reactome; R-MMU-1300642; Sperm Motility And Taxes.
DR BioGRID-ORCS; 76718; 1 hit in 58 CRISPR screens.
DR ChiTaRS; Catsperg1; mouse.
DR PRO; PR:C6KI89; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; C6KI89; protein.
DR Bgee; ENSMUSG00000049123; Expressed in spermatocyte and 9 other tissues.
DR ExpressionAtlas; C6KI89; baseline and differential.
DR Genevisible; C6KI89; MM.
DR GO; GO:0036128; C:CatSper complex; IDA:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0097228; C:sperm principal piece; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR028246; CATSPERG.
DR PANTHER; PTHR14327; PTHR14327; 1.
DR Pfam; PF15064; CATSPERG; 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; Signal; Spermatogenesis;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..1145
FT /note="Cation channel sperm-associated auxiliary subunit
FT gamma 2"
FT /id="PRO_0000388712"
FT TOPO_DOM 39..1061
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 1062..1083
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 1084..1145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34225353"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1038
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..106
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 160..166
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 289..344
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 395..403
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 634..856
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 802..830
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 878..1042
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 905..914
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT DISULFID 1006..1012
FT /evidence="ECO:0000269|PubMed:34225353,
FT ECO:0007744|PDB:7EEB"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 55..59
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 388..391
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 403..411
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 416..423
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 428..434
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 435..438
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 439..446
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 474..480
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 481..484
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 485..498
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 514..519
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 521..529
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 534..538
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 551..562
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 570..580
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 583..590
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 593..595
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 597..602
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 605..610
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 617..622
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 625..630
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 635..643
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 647..651
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 653..658
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 672..691
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 699..702
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 704..708
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 709..714
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 715..723
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 730..732
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 735..737
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 738..742
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 754..756
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 761..769
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 777..779
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 782..785
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 787..790
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 793..799
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 800..802
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 804..812
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 813..816
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 817..825
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 836..838
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 841..849
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 853..855
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 857..860
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 863..866
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 868..877
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 882..886
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 888..898
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 914..916
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 925..933
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 935..937
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 942..952
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 961..968
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 978..980
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 988..990
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 1002..1004
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 1018..1021
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 1024..1032
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 1034..1036
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 1046..1053
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 1059..1082
FT /evidence="ECO:0007829|PDB:7EEB"
SQ SEQUENCE 1145 AA; 131417 MW; 8148812F13129674 CRC64;
MVSRPAMSPV SPVWPRKPNL WAFWVLRLVL LLSLKSWAED ALQHCTWLLV LNKFEKVGLH
LSKDRFQDHE PIDTVAKVFQ KLTDSPIDPS ENYLSFPYYL QINFSCPGQN IEELARKGHL
MGMKPMVQIN YMYSVNFYRW EMENVQILME AAPMRSTGYC PAEAMCVLNW YTPMPFKNGS
VVSSVDIYTN GIGPFVSKKR FYVNMNGFLK RDASGKSLFA IGYESLVLKS SHFRLSKSRP
LWYTVNHAPV FILGGFYDEK SILFSDSNFQ DYVLLELSID SCWVGSFYCP ILGFSATIHD
AIATESTLFI RQNQLVYYFT GTYITLFDKS HGSSRWVRVL PSECIKRLCP VYASGNGSEY
VLALTTGKNE GYIHIGTITD GLVSFEMVPD GWSVCEKLPG KNCSIDWATY IADERNLLLL
VKIDSGQFYL VNFNTEFKTL NILYKIPEFI PEAKELDFLV LLDTVTYTNT PMTPKGLFFN
TLNNMLYIWG NFILQSYNRE EFIFLADFPK ESTIKYMVNS FKGQMAVVTE NEEIWYFLEG
GYDVYQVVPS QGWETYHNLQ KMQKSSFHSE DESLVSLFFE DGKLFQLVYL FDVGKERLVK
RLLPVGTLME YNLPKPFTVV NQGNYQAISF THTCPFKEIH LIDVPKKHHA SRTESYVALP
PLVSESLGFH NNNTLAVYQG LVYYLLWLHS KYDKPYADPV HDPTWRWWQH KTKDKDYFFY
LFSNRLAAEG IYINMNAYQK LYNMSGDYGI PDLFFLDKGN WFTITVVLLS HQDTFTSSDS
QGPTINVDKK LAIAVTIADP ECLSVTVTQD VLLNRNAVIN KIKVIDKKRC SEQGMIGRNI
KKTSMMLKVL GAPGNCIQRT YLGGIIQGFK VVPIFIGCPP GKRLAFDVSY TIMHSEEINK
HYFDCVIKDA EMPCFLFRDL FQPFFLVQDL VTGDSGSFLG SYVLKVVGGG RTLNTIRDYT
EEEIFRYNSP LDTTNSLIWK TKVERTTEDK KFYIMSHESP GVEWLCLENS PCYDIIPQSI
YPPEFFFKLL VSNRGVDNST YCDYKLTFIV HIHGLPLSSK RTSFIVMVST SFFIALVVFY
ILFCLVWPHI VKAWVSLRWR INNIMASESY YTYASSTAGF SLQSHSFEGP SRAGSKEDNV
QAKTA
