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CTSRD_RAT
ID   CTSRD_RAT               Reviewed;         803 AA.
AC   B5DFM7; A0A0H2UI41;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 2.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Cation channel sperm-associated auxiliary subunit delta {ECO:0000312|RGD:1594167};
DE            Short=CatSper-delta;
DE            Short=CatSperdelta;
DE   AltName: Full=Transmembrane protein 146;
DE   Flags: Precursor;
GN   Name=Catsperd {ECO:0000312|RGD:1594167}; Synonyms=Tmem146;
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] {ECO:0000312|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
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. Required for CATSPER1 stability before
CC       intraflagellar transport and/or incorporation of the CatSper complex
CC       channel into the flagellar membrane. {ECO:0000250|UniProtKB:E9Q9F6}.
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. The auxiliary CATSPERB,
CC       CATSPERG, CATSPERD and CATSPERE subunits form a pavilion-like structure
CC       over the pore which stabilizes the complex through interactions with
CC       CATSPER4, CATSPER3, CATSPER1 and CATSPER2 respectively. SLCO6C1
CC       interacts with CATSPERE and TMEM262/CATSPERH interacts with CATSPERB,
CC       further stabilizing the complex. C2CD6/CATSPERT interacts at least with
CC       CATSPERD and is required for targeting the CatSper complex in the
CC       flagellar membrane (By similarity). {ECO:0000250|UniProtKB:E9Q9F6,
CC       ECO:0000250|UniProtKB:Q91ZR5}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC       {ECO:0000250|UniProtKB:E9Q9F6}; Single-pass type I membrane protein
CC       {ECO:0000255}. Note=Specifically located in the principal piece of
CC       sperm tail. {ECO:0000250|UniProtKB:E9Q9F6}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=B5DFM7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B5DFM7-2; Sequence=VSP_061421, VSP_061422;
CC   -!- SIMILARITY: Belongs to the CATSPERD family. {ECO:0000305}.
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DR   EMBL; AABR07066520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07066522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07066521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC169121; AAI69121.1; -; mRNA.
DR   RefSeq; NP_001128456.1; NM_001134984.1.
DR   AlphaFoldDB; B5DFM7; -.
DR   STRING; 10116.ENSRNOP00000067404; -.
DR   GlyGen; B5DFM7; 2 sites.
DR   PaxDb; B5DFM7; -.
DR   GeneID; 680264; -.
DR   KEGG; rno:680264; -.
DR   CTD; 257062; -.
DR   RGD; 1594167; Catsperd.
DR   VEuPathDB; HostDB:ENSRNOG00000048818; -.
DR   eggNOG; ENOG502QSPE; Eukaryota.
DR   HOGENOM; CLU_019182_0_0_1; -.
DR   InParanoid; B5DFM7; -.
DR   OMA; QDNYSFI; -.
DR   OrthoDB; 213907at2759; -.
DR   PhylomeDB; B5DFM7; -.
DR   Reactome; R-RNO-1300642; Sperm Motility And Taxes.
DR   PRO; PR:B5DFM7; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000048818; Expressed in testis and 14 other tissues.
DR   GO; GO:0036128; C:CatSper complex; ISS:UniProtKB.
DR   GO; GO:0097228; C:sperm principal piece; ISS:UniProtKB.
DR   GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR   GO; GO:0048240; P:sperm capacitation; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   InterPro; IPR028751; CATSPERD/E.
DR   PANTHER; PTHR33722; PTHR33722; 1.
DR   Pfam; PF15020; CATSPERD; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; 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..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..803
FT                   /note="Cation channel sperm-associated auxiliary subunit
FT                   delta"
FT                   /id="PRO_0000416885"
FT   TOPO_DOM        16..720
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   TRANSMEM        721..742
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   TOPO_DOM        743..803
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   REGION          782..803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..803
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        436
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        468
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        534
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        545
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        626
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        19..365
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   DISULFID        55..142
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   DISULFID        141..148
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   DISULFID        383..492
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   DISULFID        506..698
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   DISULFID        521..568
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   DISULFID        620..648
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   VAR_SEQ         696..713
FT                   /note="SYCDLNTIFSVYVYGALP -> RYSSTAQGSAPVLGFGAK (in isoform
FT                   2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_061421"
FT   VAR_SEQ         714..803
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_061422"
SQ   SEQUENCE   803 AA;  91436 MW;  184B06F1236145C5 CRC64;
     MLMLMLAAVA TVVRAQTVCR FRTVRTGKVF ANPVTLEGDL LFYAFSNTVV VKNVCKTDIA
     VYLGQRVFIT KNRFEASILP LTIPKSMEVK MPSITSAHFV SDAMILFVID GKVYSYNFIE
     DIWRTVNGIT EPVSHISGDP CCFEGYFCLE LSNNLFAYFR GGQMPGTNIY FSNNGGFSFE
     LLNSDRMSHL KGLLGGIFHF HSLSQVGILL VENNLGTFHY LEYPLNHSTG VPFLYESPLE
     VIIKPQQRGF LILWNQKTLL VSSNSGQIVE AMQLMEEGNI NDLNVEHAKL TIHSIASNTY
     ELAFLVEQDQ LYYGSQSYMG NYIIKLSNQQ FWSEEASVHF WDVGMLEVLT PVSDPYFPAF
     DFKKCLVNVQ LALMDQSLQL EPCNVEFLES TMEDRMFIID MNSKLKLSAL MVPRKGMNPT
     PLVMVSNPHA LGFKANLTQF GNMYDGNSKF KLDIELQQQQ HWGNSELNFT ASIKHEAISS
     ITVDIADKTL SCVDLKPLST LISVGCDLTK KVIVQNKISA CAMGILDPVL LQKNYSYTIE
     KEAYNPTSYS GEAQDDLIVF YQYKELGCPR LVYYDKPWKP VVELWKDGTL EEIMNAEYVI
     LELNGIVTYS YSLTAATAHC RSQPQNWSIF KEDAEKPSLW NRETYVSCHE DNQDNPLLWP
     NVEYQILGGR TDNKIIFGQR NGIYTFYLTV VDPYYSYCDL NTIFSVYVYG ALPVAEFRPM
     TSILLMVTVT LFTMWLAYAI PKQLRTERGR RLTGFCFQIF KYCPGICTCA WLRGKMRRGL
     RSRRVKDQPE KIPQIGKKPD IKK
 
 
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