CTSR2_RAT
ID CTSR2_RAT Reviewed; 584 AA.
AC Q6AXP6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cation channel sperm-associated protein 2;
DE Short=CatSper2;
GN Name=Catsper2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP TISSUE SPECIFICITY.
RX PubMed=11675491; DOI=10.1073/pnas.221454998;
RA Quill T.A., Ren D., Clapham D.E., Garbers D.L.;
RT "A voltage-gated ion channel expressed specifically in spermatozoa.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12527-12531(2001).
CC -!- FUNCTION: Voltage-gated calcium channel that plays a central role in
CC sperm cell hyperactivation. Controls calcium entry to mediate the
CC hyperactivated motility, a step needed for sperm motility which is
CC essential late in the preparation of sperm for fertilization. Activated
CC by intracellular alkalinization. {ECO:0000250|UniProtKB:A2ARP9}.
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, C2CD6/CATSPERT, SLCO6C1, TMEM249, TMEM262 and EFCAB9 (By
CC similarity). HSPA1 may be an additional auxiliary complex member (By
CC similarity). The core complex members CATSPER1, CATSPER2, CATSPER3 and
CC CATSPER4 form a heterotetrameric channel (By similarity). The auxiliary
CC CATSPERB, CATSPERG, 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 (By similarity). SLCO6C1 interacts with CATSPERE and
CC TMEM262/CATSPERH interacts with CATSPERB, further stabilizing the
CC complex. C2CD6/CATSPERT interacts at least with CATSPERD and is
CC required for targeting the CatSper complex in the flagellar membrane
CC (By similarity). Interacts with Ca(v)3.3/CACNA1I, leading to
CC suppression of T-type calcium channel activity (By similarity).
CC {ECO:0000250|UniProtKB:A2ARP9, ECO:0000250|UniProtKB:Q91ZR5,
CC ECO:0000250|UniProtKB:Q96P56}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000250|UniProtKB:A2ARP9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:A2ARP9}.
CC -!- SIMILARITY: Belongs to the cation channel sperm-associated (TC
CC 1.A.1.19) family. {ECO:0000305}.
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DR EMBL; BC079422; AAH79422.1; -; mRNA.
DR RefSeq; NP_001012220.1; NM_001012220.1.
DR RefSeq; XP_008760409.1; XM_008762187.2.
DR RefSeq; XP_017447438.1; XM_017591949.1.
DR AlphaFoldDB; Q6AXP6; -.
DR SMR; Q6AXP6; -.
DR STRING; 10116.ENSRNOP00000038712; -.
DR PhosphoSitePlus; Q6AXP6; -.
DR PaxDb; Q6AXP6; -.
DR Ensembl; ENSRNOT00000030019; ENSRNOP00000038712; ENSRNOG00000023064.
DR GeneID; 366174; -.
DR KEGG; rno:366174; -.
DR UCSC; RGD:1307620; rat.
DR CTD; 117155; -.
DR RGD; 1307620; Catsper2.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00910000144338; -.
DR HOGENOM; CLU_038828_0_0_1; -.
DR InParanoid; Q6AXP6; -.
DR OMA; GWVLECK; -.
DR OrthoDB; 580290at2759; -.
DR PhylomeDB; Q6AXP6; -.
DR TreeFam; TF343585; -.
DR Reactome; R-RNO-1300642; Sperm Motility And Taxes.
DR PRO; PR:Q6AXP6; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000023064; Expressed in testis and 20 other tissues.
DR Genevisible; Q6AXP6; RN.
DR GO; GO:0036128; C:CatSper complex; ISS:UniProtKB.
DR GO; GO:0036126; C:sperm flagellum; ISO:RGD.
DR GO; GO:0005227; F:calcium activated cation channel activity; IEA:InterPro.
DR GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0009566; P:fertilization; ISO:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0048240; P:sperm capacitation; ISO:RGD.
DR Gene3D; 1.20.120.350; -; 1.
DR InterPro; IPR028747; CatSper2.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR46923; PTHR46923; 1.
DR Pfam; PF00520; Ion_trans; 1.
PE 2: Evidence at transcript level;
KW Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Cell projection; Cilium; Developmental protein; Differentiation; Flagellum;
KW Ion channel; Ion transport; Membrane; Reference proteome; Spermatogenesis;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..584
FT /note="Cation channel sperm-associated protein 2"
FT /id="PRO_0000295678"
FT TOPO_DOM 1..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT TRANSMEM 107..129
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT TOPO_DOM 130..138
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT TRANSMEM 139..164
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT TOPO_DOM 165..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT TRANSMEM 174..198
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT TOPO_DOM 199..201
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT TRANSMEM 202..220
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT TOPO_DOM 221..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT TRANSMEM 238..260
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT TOPO_DOM 261..279
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT INTRAMEM 280..292
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT TOPO_DOM 293..312
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT TRANSMEM 313..339
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT TOPO_DOM 340..584
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A2ARP9"
FT REGION 376..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..414
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..444
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 68266 MW; 36E0993AF87E5233 CRC64;
MAHERGHLQL PRADAIRSKL IDTFSLIEHL QGLSQAVPRH TLREILDPAC QKKLMLGDQE
QLVRFSIRAR RMGHITHAQR LLSRLRVRCG GRPPLSLWAG WVLDSSIFSN FIISLIFLNT
FVLMVEIELM NSTNTSLWPL KLALEVTDWF ILLSFIVEIL LMWLASFFLF WKNAWSVFDF
VVTMLSLLPE FVVLIGVSAD SVWLQLLRVS RVLRSLKLFA RFPQIKVILL ALVRALKSMT
FLLMLLLIFF YVFAVAGVYF FKEYSRSTIE NLEYNMFFSD LLNSLVTVFI LFTLDHWYAV
LQDVWKVPEA SRVFSSIYVI LWLLLGSIIF RNIIVAMMVT NFQNIRNELH EEMTHLEVQY
KADIFKRRII QRRQQSESLR GTSQGKVSED ITETSEATDE EKSEAEESEE EKSEEEKSDV
EKSDEEKNDE EKSDEEENDE EKSDVEKSDE EKNDEEKGYT EKVYSGRTFV ERSYAERSFA
GKAENEKVQK ELKEKAYPGS PPNSSSHDEA FAADDTYLEN LDWETLVHEN LPGLMDMDQD
DRVVWPRDSL FRYFELLESL QYNLEERKRL QEFAVQALMN FEDK
