CTSRG_MACFA
ID CTSRG_MACFA Reviewed; 1159 AA.
AC Q4R6B2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Cation channel sperm-associated auxiliary subunit gamma {ECO:0000250|UniProtKB:Q6ZRH7};
DE Flags: Precursor;
GN Name=CATSPERG {ECO:0000250|UniProtKB:Q6ZRH7}; ORFNames=QtsA-18551;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Auxiliary component of the CatSper complex, a complex
CC involved in sperm cell hyperactivation. Sperm cell hyperactivation is
CC needed for sperm motility which is essential late in the preparation of
CC sperm for fertilization. {ECO:0000250|UniProtKB:C6KI89}.
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, CATSPERG, CATSPERD, CATSPERE,
CC CATSPERZ, SCLO6C1, TMEM249, TMEM262 and EFCAB9. HSPA1 may be an
CC additional auxiliary complex member. The core complex members CATSPER1,
CC CATSPER2, CATSPER3 and CATSPER4 form a heterotetrameric channel. The
CC auxiliary CATSPERB, CATSPERG, CATSPERD and CATSPERE subunits form a
CC pavilion-like structure over the pore which stabilizes the complex
CC through interactions with CATSPER4, CATSPER3, CATSPER1 and CATSPER2
CC respectively. TMEM262/CATSPERH interacts with CATSPERB, further
CC stabilizing the complex. C2CD6/CATSPERT interacts at least with
CC CATSPERD and is required for targeting the CatSper complex in the
CC flagellar membrane. {ECO:0000250|UniProtKB:C6KI89}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CATSPERG family. {ECO:0000305}.
CC -!- CAUTION: In mouse, Slco6c1 is an additional auxiliary subunit of the
CC CatSper complex. It is unclear if the related SLCO6A1 protein performs
CC the same role in non-rodent species. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB169275; BAE01363.1; -; mRNA.
DR RefSeq; NP_001306307.1; NM_001319378.1.
DR AlphaFoldDB; Q4R6B2; -.
DR SMR; Q4R6B2; -.
DR STRING; 9541.XP_005589154.1; -.
DR PRIDE; Q4R6B2; -.
DR GeneID; 102116738; -.
DR CTD; 57828; -.
DR eggNOG; ENOG502QWAR; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0036128; C:CatSper complex; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cilium; Developmental protein;
KW Differentiation; Disulfide bond; Flagellum; Glycoprotein; Membrane;
KW Reference proteome; Signal; Spermatogenesis; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1159
FT /note="Cation channel sperm-associated auxiliary subunit
FT gamma"
FT /id="PRO_0000019566"
FT TOPO_DOM 36..1065
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:C6KI89"
FT TRANSMEM 1066..1087
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:C6KI89"
FT TOPO_DOM 1088..1159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:C6KI89"
FT REGION 1138..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..105
FT /evidence="ECO:0000250|UniProtKB:C6KI89"
FT DISULFID 159..165
FT /evidence="ECO:0000250|UniProtKB:C6KI89"
FT DISULFID 288..343
FT /evidence="ECO:0000250|UniProtKB:C6KI89"
FT DISULFID 394..402
FT /evidence="ECO:0000250|UniProtKB:C6KI89"
FT DISULFID 638..860
FT /evidence="ECO:0000250|UniProtKB:C6KI89"
FT DISULFID 806..834
FT /evidence="ECO:0000250|UniProtKB:C6KI89"
FT DISULFID 882..1046
FT /evidence="ECO:0000250|UniProtKB:C6KI89"
FT DISULFID 909..918
FT /evidence="ECO:0000250|UniProtKB:C6KI89"
FT DISULFID 1010..1016
FT /evidence="ECO:0000250|UniProtKB:C6KI89"
SQ SEQUENCE 1159 AA; 133551 MW; CF9840A8FE3E10CF CRC64;
MCGPAMFPAG PRWPRVRVLQ VLWALLAVLL ASRRLWAIKD FEECTWQVVL NEFKRVGENG
ASDRFFEQEL VDTVGNLFHM LVDSPIDPRE KYLGFPYYLK INYSCEEKHS EDLVRMGHLT
GLKPVVLVTF QSPVNFYRWK IEQLQIQMEA APFRSKEPCI AEEVCSMSWY TPMPIKNGSV
VTRVDVSSNG LGTFIPDKRF QVNINGFLKR NQDNDIQFTV GDELFNLMPQ YFVGISSRPL
WHTVDQSPVL ILGGIPNEKY VLMTDTSFKD FSLVELSIDS CWVGSFYCPQ SGFTATIYDT
VATESTLFIR QNQLVYYFTG TYTTLYERNR GSGSWVRVLA SECIKKLCPV YFHSNGSEYI
MALTTGKHEG FVHFGTIRDG QVSFEMLPRE WSVCEQIGVT TCSIIWSDYI AGEYTLLLLV
ESEYENASKR FQVVSYNTAN DDLELLYHIP EFIPEARGLE FLMILGTESY TNTVMTPKGI
SCNPYNHLIF IWGNFLLQSS NKENFIYLAD FPKELSIKYM TRSFRGAVAI VTETEEIWYL
LEGTYRVYRL FPSKGWKVHI SLQLMQQSSL YASNETMLTL FYEGSKLYQL VYLMNNQKGQ
LVKRLMPVEQ LLMYQQHTSH YDLDRKGGYL MLSFTNFCPF SVMRLRNLPG PQRYTRQERY
RARPPHVLER SGFHNENSLA IYQGLIYYLL WLHSVYDKPY ADPVHDPTWR WWENNKQDQD
YYFFLASNWR SAGGVFIEMD SYEKIYNLKS AYELPERIFL DKGTEYSFAI FLSAQSRSFR
TMADLGTVFE LHSHVDVGVV LADPGCIEAS VKQEVLINRN AVLFSITLKD KKVCYDQGIS
GHHLMKSSMT VNVVGSSGLC FQETHAGARM QGNLMVPVFI GCPPGKRLAF DITYTLEYSR
LKNKHYFDCV QVDPEMPCFL FRDIFYPFFL IQDLVTGDSG SFQGSYVLLV VGGGPTLDTL
KDYNKDEIYR FNSPLDKTHS LIWTTRTKRT TKDSAFHIMS HESPGIEWLC LENAPCYDNV
PQGIFAPEFF FKVLVSNRGV DTSTYCNYQL TFLLHIHGLP LSPKRALFIL MVSLSVFVGL
VIFYIAFCLL WPLVVKGCTM IRWKINDIIA SESYYTYASI SGMSSMQSLR RSRMGSMFSS
RMTEDKAEPK EAVERQLMT
