位置:首页 > 蛋白库 > CTSR3_MOUSE
CTSR3_MOUSE
ID   CTSR3_MOUSE             Reviewed;         395 AA.
AC   Q80W99; Q5FWA9; Q9D5T9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Cation channel sperm-associated protein 3;
DE            Short=CatSper3;
GN   Name=Catsper3;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, INTERACTION WITH CATSPER1, AND DISRUPTION PHENOTYPE.
RC   STRAIN=BALB/cJ; TISSUE=Testis;
RX   PubMed=17227845; DOI=10.1073/pnas.0610286104;
RA   Qi H., Moran M.M., Navarro B., Chong J.A., Krapivinsky G., Krapivinsky L.,
RA   Kirichok Y., Ramsey I.S., Quill T.A., Clapham D.E.;
RT   "All four CatSper ion channel proteins are required for male fertility and
RT   sperm cell hyperactivated motility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1219-1223(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [4]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16107607; DOI=10.1095/biolreprod.105.045468;
RA   Jin J.-L., O'Doherty A.M., Wang S., Zheng H., Sanders K.M., Yan W.;
RT   "Catsper3 and catsper4 encode two cation channel-like proteins exclusively
RT   expressed in the testis.";
RL   Biol. Reprod. 73:1235-1242(2005).
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17347248; DOI=10.1093/molehr/gam009;
RA   Li H.-G., Ding X.-F., Liao A.-H., Kong X.-B., Xiong C.-L.;
RT   "Expression of CatSper family transcripts in the mouse testis during post-
RT   natal development and human ejaculated spermatozoa: relationship to sperm
RT   motility.";
RL   Mol. Hum. Reprod. 13:299-306(2007).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17344468; DOI=10.1095/biolreprod.107.060186;
RA   Jin J.-L., Jin N., Zheng H., Ro S., Tafolla D., Sanders K.M., Yan W.;
RT   "Catsper3 and catsper4 are essential for sperm hyperactivated motility and
RT   male fertility in the mouse.";
RL   Biol. Reprod. 77:37-44(2007).
RN   [7]
RP   LACK OF ACTIVATION BY PROGESTERONE AND PGE1.
RX   PubMed=21412339; DOI=10.1038/nature09767;
RA   Lishko P.V., Botchkina I.L., Kirichok Y.;
RT   "Progesterone activates the principal Ca2+ channel of human sperm.";
RL   Nature 471:387-391(2011).
RN   [8]
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   [9]
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   [10]
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) OF THE CATSPER COMPLEX,
RP   IDENTIFICATION BY MASS SPECTROMETRY, TRANSMEMBRANE DOMAINS, AND TOPOLOGY.
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: 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:0000269|PubMed:17227845,
CC       ECO:0000269|PubMed:17344468}.
CC   -!- ACTIVITY REGULATION: In contrast to the human ortholog, not activated
CC       by progesterone. {ECO:0000269|PubMed:21412339}.
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:17227845, PubMed:21224844, PubMed:34998468).
CC       HSPA1 may be an additional auxiliary complex member (By similarity).
CC       The core complex members CATSPER1, CATSPER2, CATSPER3 and CATSPER4 form
CC       a 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:17227845, ECO:0000269|PubMed:21224844,
CC       ECO:0000269|PubMed:34225353, ECO:0000269|PubMed:34998468}.
CC   -!- INTERACTION:
CC       Q80W99; Q91ZR5: Catsper1; NbExp=2; IntAct=EBI-15619135, EBI-15619083;
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC       {ECO:0000269|PubMed:16107607, ECO:0000269|PubMed:17227845}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:34225353}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80W99-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80W99-2; Sequence=VSP_026978;
CC   -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:16107607,
CC       ECO:0000269|PubMed:17227845}.
CC   -!- DEVELOPMENTAL STAGE: Detected in hte testis during postnatal
CC       development at day 15. Restricted to the late-stage germline cells that
CC       line the seminiferous tubules. {ECO:0000269|PubMed:17347248}.
CC   -!- DISRUPTION PHENOTYPE: Mice are normal but males are sterile. Male
CC       sterility is due to defects in sperm motility unability to fertilize
CC       intact eggs. {ECO:0000269|PubMed:17227845,
CC       ECO:0000269|PubMed:17344468}.
CC   -!- SIMILARITY: Belongs to the cation channel sperm-associated (TC
CC       1.A.1.19) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH89518.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={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; AY263400; AAP21831.1; -; mRNA.
DR   EMBL; AK014942; BAB29631.1; -; mRNA.
DR   EMBL; BC089518; AAH89518.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS26555.1; -. [Q80W99-2]
DR   CCDS; CCDS56885.1; -. [Q80W99-1]
DR   RefSeq; NP_001239416.1; NM_001252487.1. [Q80W99-1]
DR   RefSeq; NP_084048.1; NM_029772.4. [Q80W99-2]
DR   RefSeq; XP_006517518.1; XM_006517455.2. [Q80W99-1]
DR   PDB; 7EEB; EM; 2.90 A; C=1-395.
DR   PDBsum; 7EEB; -.
DR   AlphaFoldDB; Q80W99; -.
DR   SMR; Q80W99; -.
DR   BioGRID; 218352; 2.
DR   CORUM; Q80W99; -.
DR   DIP; DIP-60802N; -.
DR   IntAct; Q80W99; 1.
DR   STRING; 10090.ENSMUSP00000021961; -.
DR   GuidetoPHARMACOLOGY; 390; -.
DR   TCDB; 1.A.1.19.3; the voltage-gated ion channel (vic) superfamily.
DR   PhosphoSitePlus; Q80W99; -.
DR   jPOST; Q80W99; -.
DR   PaxDb; Q80W99; -.
DR   PRIDE; Q80W99; -.
DR   ProteomicsDB; 285427; -. [Q80W99-1]
DR   ProteomicsDB; 285428; -. [Q80W99-2]
DR   Antibodypedia; 26383; 66 antibodies from 16 providers.
DR   DNASU; 76856; -.
DR   Ensembl; ENSMUST00000021961; ENSMUSP00000021961; ENSMUSG00000021499. [Q80W99-1]
DR   Ensembl; ENSMUST00000109898; ENSMUSP00000105524; ENSMUSG00000021499. [Q80W99-2]
DR   GeneID; 76856; -.
DR   KEGG; mmu:76856; -.
DR   UCSC; uc007qsb.2; mouse. [Q80W99-2]
DR   UCSC; uc007qsc.2; mouse. [Q80W99-1]
DR   CTD; 347732; -.
DR   MGI; MGI:1924106; Catsper3.
DR   VEuPathDB; HostDB:ENSMUSG00000021499; -.
DR   eggNOG; KOG2302; Eukaryota.
DR   GeneTree; ENSGT00940000161455; -.
DR   HOGENOM; CLU_058058_0_0_1; -.
DR   InParanoid; Q80W99; -.
DR   OMA; YTLFQVM; -.
DR   PhylomeDB; Q80W99; -.
DR   TreeFam; TF343841; -.
DR   Reactome; R-MMU-1300642; Sperm Motility And Taxes.
DR   BioGRID-ORCS; 76856; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; Catsper3; mouse.
DR   PRO; PR:Q80W99; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q80W99; protein.
DR   Bgee; ENSMUSG00000021499; Expressed in spermatid and 12 other tissues.
DR   ExpressionAtlas; Q80W99; baseline and differential.
DR   Genevisible; Q80W99; MM.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR   GO; GO:0036128; C:CatSper complex; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR   GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IMP:MGI.
DR   GO; GO:0048240; P:sperm capacitation; IMP:MGI.
DR   Gene3D; 1.20.120.350; -; 1.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   Pfam; PF00520; Ion_trans; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Calcium channel;
KW   Calcium transport; Cell membrane; Cell projection; Cilium;
KW   Developmental protein; Differentiation; Flagellum; Ion channel;
KW   Ion transport; Membrane; Reference proteome; Spermatogenesis;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..395
FT                   /note="Cation channel sperm-associated protein 3"
FT                   /id="PRO_0000295680"
FT   TOPO_DOM        1..48
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   TRANSMEM        49..71
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   TOPO_DOM        72..80
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   TRANSMEM        81..107
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   TOPO_DOM        108
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   TRANSMEM        109..131
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   TOPO_DOM        132..143
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   TRANSMEM        144..160
FT                   /note="Helical; Name=Segment S4"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   TOPO_DOM        161..168
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   TRANSMEM        169..195
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   TOPO_DOM        196..216
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   INTRAMEM        217..236
FT                   /note="Helical; Pore-forming"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   TOPO_DOM        237..242
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   TRANSMEM        243..268
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   TOPO_DOM        269..395
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:34225353"
FT   VAR_SEQ         84..96
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_026978"
FT   CONFLICT        314
FT                   /note="S -> T (in Ref. 1; AAP21831)"
FT                   /evidence="ECO:0000305"
FT   HELIX           39..47
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   HELIX           50..69
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   HELIX           73..77
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   HELIX           80..103
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   HELIX           108..110
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   HELIX           113..133
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   HELIX           142..147
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   HELIX           148..158
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   HELIX           161..171
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   HELIX           174..199
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   TURN            200..202
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   STRAND          203..205
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   TURN            207..209
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   STRAND          210..212
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   HELIX           213..224
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   HELIX           229..237
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   HELIX           244..255
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   TURN            256..259
FT                   /evidence="ECO:0007829|PDB:7EEB"
FT   HELIX           260..314
FT                   /evidence="ECO:0007829|PDB:7EEB"
SQ   SEQUENCE   395 AA;  45486 MW;  10641E91039210A6 CRC64;
     MSQHFHHNPV RVKSGSLFAT ASEALQARLS KIKRKDKECQ AYFRKVIKST FFQIVMITTV
     TTNSFLLVLG TNYDIQFEFF RTFEVSELFF VSVYVCEFLM KVYVDPITYW KDGYNILDVI
     ILIILTIPYL LRKIKGNHSA YLHFADGIQS LRILKLISYS RGIRTLIIAV GETVYTVASV
     LTLLFLLMFV FAILGFCLFG VTDRGDLENW GNLASAFFTL FSLATVDGWT DLQEELDKRK
     FTVSRAFTIL FILLASFIFL NMFVGVMIMH TEDSMKKFER DLTLERNLAI MEEKQIILKR
     QQEEVNRLMN TQKSGSMNFI DMVEGFKKTL RHTDPMVLDD FSTSLSFIDI YLVTLDNQDV
     IVSKLQELYC EIVNVLSLML EDMPKESSSS LSGLS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024