CTSRB_HUMAN
ID CTSRB_HUMAN Reviewed; 1116 AA.
AC Q9H7T0; A0AV51;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cation channel sperm-associated auxiliary subunit beta {ECO:0000312|HGNC:HGNC:20500};
DE Short=CatSper-beta;
GN Name=CATSPERB {ECO:0000312|HGNC:HGNC:20500};
GN Synonyms=C14orf161 {ECO:0000312|HGNC:HGNC:20500};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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. {ECO:0000250|UniProtKB:A2RTF1}.
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, 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:A2RTF1}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000250|UniProtKB:A2RTF1}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:A2RTF1}. Note=Predominantly located in the
CC principal piece of the sperm tail. {ECO:0000250|UniProtKB:A2RTF1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H7T0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H7T0-2; Sequence=VSP_027008;
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}.
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DR EMBL; AK024360; BAB14896.1; -; mRNA.
DR EMBL; BC126214; AAI26215.1; -; mRNA.
DR EMBL; BC126216; AAI26217.1; -; mRNA.
DR CCDS; CCDS32142.1; -. [Q9H7T0-1]
DR RefSeq; NP_079040.2; NM_024764.3. [Q9H7T0-1]
DR AlphaFoldDB; Q9H7T0; -.
DR SMR; Q9H7T0; -.
DR BioGRID; 122915; 1.
DR STRING; 9606.ENSP00000256343; -.
DR TCDB; 1.A.1.19.1; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; Q9H7T0; 5 sites.
DR iPTMnet; Q9H7T0; -.
DR PhosphoSitePlus; Q9H7T0; -.
DR BioMuta; CATSPERB; -.
DR DMDM; 158519875; -.
DR EPD; Q9H7T0; -.
DR jPOST; Q9H7T0; -.
DR MassIVE; Q9H7T0; -.
DR PaxDb; Q9H7T0; -.
DR PeptideAtlas; Q9H7T0; -.
DR PRIDE; Q9H7T0; -.
DR ProteomicsDB; 81144; -. [Q9H7T0-1]
DR Antibodypedia; 49510; 43 antibodies from 16 providers.
DR DNASU; 79820; -.
DR Ensembl; ENST00000256343.8; ENSP00000256343.3; ENSG00000133962.8. [Q9H7T0-1]
DR Ensembl; ENST00000619027.2; ENSP00000478546.1; ENSG00000274338.2. [Q9H7T0-1]
DR GeneID; 79820; -.
DR KEGG; hsa:79820; -.
DR MANE-Select; ENST00000256343.8; ENSP00000256343.3; NM_024764.4; NP_079040.2.
DR UCSC; uc001xzs.2; human. [Q9H7T0-1]
DR CTD; 79820; -.
DR DisGeNET; 79820; -.
DR GeneCards; CATSPERB; -.
DR HGNC; HGNC:20500; CATSPERB.
DR HPA; ENSG00000133962; Tissue enriched (pancreas).
DR MIM; 611169; gene.
DR neXtProt; NX_Q9H7T0; -.
DR OpenTargets; ENSG00000133962; -.
DR PharmGKB; PA162381112; -.
DR VEuPathDB; HostDB:ENSG00000133962; -.
DR eggNOG; ENOG502QZ5S; Eukaryota.
DR GeneTree; ENSGT00390000008198; -.
DR HOGENOM; CLU_012454_0_0_1; -.
DR InParanoid; Q9H7T0; -.
DR OMA; KEPFLEW; -.
DR PhylomeDB; Q9H7T0; -.
DR TreeFam; TF328432; -.
DR PathwayCommons; Q9H7T0; -.
DR Reactome; R-HSA-1300642; Sperm Motility And Taxes.
DR BioGRID-ORCS; 79820; 11 hits in 1073 CRISPR screens.
DR ChiTaRS; CATSPERB; human.
DR GenomeRNAi; 79820; -.
DR Pharos; Q9H7T0; Tdark.
DR PRO; PR:Q9H7T0; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9H7T0; protein.
DR Bgee; ENSG00000133962; Expressed in body of pancreas and 86 other tissues.
DR ExpressionAtlas; Q9H7T0; baseline and differential.
DR Genevisible; Q9H7T0; HS.
DR GO; GO:0036128; C:CatSper complex; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0097228; C:sperm principal piece; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR028748; CATSPERB.
DR PANTHER; PTHR14705; PTHR14705; 1.
DR Pfam; PF15149; CATSPERB; 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; Spermatogenesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1116
FT /note="Cation channel sperm-associated auxiliary subunit
FT beta"
FT /id="PRO_0000089953"
FT TOPO_DOM 1..1053
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:A2RTF1"
FT TRANSMEM 1054..1076
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:A2RTF1"
FT TOPO_DOM 1077..1116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:A2RTF1"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 913
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..60
FT /evidence="ECO:0000250|UniProtKB:A2RTF1"
FT DISULFID 189..302
FT /evidence="ECO:0000250|UniProtKB:A2RTF1"
FT DISULFID 330..343
FT /evidence="ECO:0000250|UniProtKB:A2RTF1"
FT DISULFID 718..816
FT /evidence="ECO:0000250|UniProtKB:A2RTF1"
FT DISULFID 829..1037
FT /evidence="ECO:0000250|UniProtKB:A2RTF1"
FT DISULFID 911..920
FT /evidence="ECO:0000250|UniProtKB:A2RTF1"
FT DISULFID 922..937
FT /evidence="ECO:0000250|UniProtKB:A2RTF1"
FT VAR_SEQ 1..478
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027008"
FT VARIANT 318
FT /note="F -> Y (in dbSNP:rs57706558)"
FT /id="VAR_061634"
SQ SEQUENCE 1116 AA; 126924 MW; 3A5DB4D5E2C1C81E CRC64;
MESPLIYVSV LLLNIFEFSS GIVYNKDDTE KRFACSNKGF PQENEIIKLY LFLENLKIQC
FFQTENEIAS KAMLSVFTSG GLAPSLGIMN STYNGIFHFN LTLFSDRILW LVDIPRENIT
QSTDIAAVEE WLVRITLHHG LNIYATEGTL LDVIREPILQ WTPGDVIPES EISKLYPHVV
DLKVTKCPCA NDVALLGFIV DTIVDGVYIG ITFGGFWHDY DTTWFNMTQT IYSQLQEEYE
DLSLVDMVLT NHFLVILTSL GLFVSEDLRY PSRHSLSFSR ADFCGFERVD YVKGKLWYNE
RCFANREHFE VDYVTVTFER NRTLSESSSC FYSQEPFLEW VPCLPHIFKG IKIFPTVLTF
LVDQERGTGV YLFYNKVRKT AIASVSTLRN NEPNSQSKFP IFRFPSSFSS PVGMVFHPRS
HFLYAYGNQI WLSVDGGNTF QLIANFHDDI IKKTFHSFYT SAITFVSQRG KVYSTKAGMG
RYSAVGSVTE RIFTLYYDHL GFLHKLTLGR FEASGPPTAF GNSRNLFGQP PDMGFETALA
PQHTSLDEII FFAYVPENEP QETIYSKKFG NIHYGKVIHS GKTGRAYIRK VLQHTTPKGF
LSSVIAEMKE PFGLEEVNES SCLSSSLLIN KAGNVYKLTL DSQVVQALFE DTDIEKTVVL
PGYSSFLITS ILDNKNALAI ATMPESAPNN MTFLKSTWFL YNFGQRNGRT WKIYSKPCNY
WFQHDDSPSL NIVKYIDLGN SYVLKAKVIR NAKGFRMLEI PLLTVFVGNP NLLEVTAEVT
FDDTDSYVIT ISAASKVLHQ GSTSLAFIMW SASTECFVTT MVPTLKSSCS YLRSMHHIPS
KFIPFEDWIS GVHKDSQGFN LIKTLPINYR PPSNMGIAIP LTDNFYHADP SKPIPRNMFH
MSKKTGKFKQ CANVSTREEC NCTKDQKFSH AVAFSDCREK VPRFKFPITQ YPVSLEIINE
DGRVPLQSPY LVTVTEVNMR HNWKLKHTVP ENIKRMKQLV EPILGAAVYN PSGLNLSIKG
SELFHFRVTV ISGVTFCNLI EEFQIYVDEA PLPFPGHTLI AVATAVVLGG LIFIAFMFQL
QGIHPWRTFQ RWIRRNQEKF SSISLSELIH RSKSEE
