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   27-MAR-2024, entry version 153.
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   GlyCosmos; Q9H7T0; 11 sites, No reported glycans.
DR   GlyGen; Q9H7T0; 11 sites.
DR   iPTMnet; Q9H7T0; -.
DR   PhosphoSitePlus; Q9H7T0; -.
DR   BioMuta; CATSPERB; -.
DR   DMDM; 158519875; -.
DR   EPD; Q9H7T0; -.
DR   jPOST; Q9H7T0; -.
DR   MassIVE; Q9H7T0; -.
DR   PaxDb; 9606-ENSP00000256343; -.
DR   PeptideAtlas; Q9H7T0; -.
DR   ProteomicsDB; 81144; -. [Q9H7T0-1]
DR   ProteomicsDB; 81145; -. [Q9H7T0-2]
DR   Antibodypedia; 49510; 54 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   AGR; HGNC:20500; -.
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   OrthoDB; 2904310at2759; -.
DR   PhylomeDB; Q9H7T0; -.
DR   TreeFam; TF328432; -.
DR   PathwayCommons; Q9H7T0; -.
DR   Reactome; R-HSA-1300642; Sperm Motility And Taxes.
DR   BioGRID-ORCS; 79820; 13 hits in 1151 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 87 other cell types or tissues.
DR   ExpressionAtlas; Q9H7T0; baseline and differential.
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   InterPro; IPR048786; CATSPERB_1st.
DR   InterPro; IPR048788; CATSPERB_2nd.
DR   InterPro; IPR048789; CATSPERB_C.
DR   PANTHER; PTHR14705:SF0; CATION CHANNEL SPERM-ASSOCIATED AUXILIARY SUBUNIT BETA; 1.
DR   PANTHER; PTHR14705; CATION CHANNEL SPERM-ASSOCIATED PROTEIN SUBUNIT BETA; 1.
DR   Pfam; PF15149; CATSPERB; 1.
DR   Pfam; PF21541; CATSPERB_1st; 1.
DR   Pfam; PF21548; CATSPERB_2nd; 1.
DR   Genevisible; Q9H7T0; HS.
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
//