TM262_HUMAN
ID TM262_HUMAN Reviewed; 116 AA.
AC E9PQX1;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Cation channel sperm-associated auxiliary subunit TMEM262 {ECO:0000305};
DE AltName: Full=Cation channel sperm-associated auxiliary subunit eta {ECO:0000250|UniProtKB:D3Z338};
DE AltName: Full=Transmembrane protein 262 {ECO:0000312|HGNC:HGNC:49389};
GN Name=TMEM262 {ECO:0000312|HGNC:HGNC:49389};
GN Synonyms=CATSPERH {ECO:0000250|UniProtKB:D3Z338};
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 GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-101.
RC TISSUE=Testis;
RA Arakawa T., Carninci P., Fukuda S., Hasegawa A., Hayashida K., Hori F.,
RA Kai C., Kawai J., Kojima M., Murata M., Nakamura M., Nishiyori H.,
RA Nomura K., Ohno M., Sasaki D., Shibazaki E., Tagami M., Tagami Y.,
RA Hayashizaki Y.;
RT "RIKEN full-length enriched human cDNA library.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Auxiliary component of the CatSper complex, a complex
CC involved in sperm cell hyperactivation. {ECO:0000250|UniProtKB:D3Z338}.
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 (By similarity).
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. The auxiliary CATSPERB, CATSPERG, CATSPERD
CC and CATSPERE subunits form a pavilion-like structure over the pore
CC which stabilizes the complex through interactions with CATSPER4,
CC CATSPER3, CATSPER1 and CATSPER2 respectively. TMEM262/CATSPERH
CC interacts with CATSPERB, further stabilizing the complex.
CC C2CD6/CATSPERT interacts at least with CATSPERD and is required for
CC targeting the CatSper complex in the flagellar membrane (By
CC similarity). {ECO:0000250|UniProtKB:D3Z338,
CC ECO:0000250|UniProtKB:Q91ZR5}.
CC -!- INTERACTION:
CC E9PQX1; Q13520: AQP6; NbExp=3; IntAct=EBI-17180389, EBI-13059134;
CC E9PQX1; P09693: CD3G; NbExp=3; IntAct=EBI-17180389, EBI-3862428;
CC E9PQX1; P11912: CD79A; NbExp=3; IntAct=EBI-17180389, EBI-7797864;
CC E9PQX1; Q9HAV5: EDA2R; NbExp=3; IntAct=EBI-17180389, EBI-526033;
CC E9PQX1; P54849: EMP1; NbExp=3; IntAct=EBI-17180389, EBI-4319440;
CC E9PQX1; O15552: FFAR2; NbExp=3; IntAct=EBI-17180389, EBI-2833872;
CC E9PQX1; O15529: GPR42; NbExp=3; IntAct=EBI-17180389, EBI-18076404;
CC E9PQX1; P26715: KLRC1; NbExp=3; IntAct=EBI-17180389, EBI-9018187;
CC E9PQX1; Q9NQG1: MANBAL; NbExp=3; IntAct=EBI-17180389, EBI-3867271;
CC E9PQX1; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-17180389, EBI-18037857;
CC E9PQX1; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-17180389, EBI-18159983;
CC E9PQX1; O75841: UPK1B; NbExp=3; IntAct=EBI-17180389, EBI-12237619;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:D3Z338}.
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; AP003068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; HY032040; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS60845.1; -.
DR RefSeq; NP_001269377.1; NM_001282448.1.
DR AlphaFoldDB; E9PQX1; -.
DR SMR; E9PQX1; -.
DR BioGRID; 934641; 14.
DR IntAct; E9PQX1; 12.
DR STRING; 9606.ENSP00000432459; -.
DR BioMuta; TMEM262; -.
DR MassIVE; E9PQX1; -.
DR PaxDb; E9PQX1; -.
DR PeptideAtlas; E9PQX1; -.
DR PRIDE; E9PQX1; -.
DR DNASU; 100130348; -.
DR Ensembl; ENST00000530719.6; ENSP00000432459.1; ENSG00000187066.9.
DR GeneID; 100130348; -.
DR KEGG; hsa:100130348; -.
DR MANE-Select; ENST00000530719.6; ENSP00000432459.1; NM_001282448.2; NP_001269377.1.
DR UCSC; uc031xrs.2; human.
DR CTD; 100130348; -.
DR GeneCards; TMEM262; -.
DR HGNC; HGNC:49389; TMEM262.
DR HPA; ENSG00000187066; Tissue enriched (testis).
DR neXtProt; NX_E9PQX1; -.
DR OpenTargets; ENSG00000187066; -.
DR VEuPathDB; HostDB:ENSG00000187066; -.
DR eggNOG; ENOG502S7IB; Eukaryota.
DR GeneTree; ENSGT00530000064783; -.
DR HOGENOM; CLU_160801_0_0_1; -.
DR InParanoid; E9PQX1; -.
DR OMA; DKFLRCF; -.
DR OrthoDB; 1596404at2759; -.
DR PhylomeDB; E9PQX1; -.
DR PathwayCommons; E9PQX1; -.
DR SignaLink; E9PQX1; -.
DR BioGRID-ORCS; 100130348; 8 hits in 962 CRISPR screens.
DR ChiTaRS; TMEM262; human.
DR GenomeRNAi; 100130348; -.
DR Pharos; E9PQX1; Tdark.
DR PRO; PR:E9PQX1; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; E9PQX1; protein.
DR Bgee; ENSG00000187066; Expressed in endometrium epithelium and 138 other tissues.
DR ExpressionAtlas; E9PQX1; baseline and differential.
DR GO; GO:0036128; C:CatSper complex; ISS:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR InterPro; IPR040431; TM262.
DR PANTHER; PTHR37998; PTHR37998; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cilium; Flagellum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..116
FT /note="Cation channel sperm-associated auxiliary subunit
FT TMEM262"
FT /id="PRO_0000424961"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:D3Z338"
FT TRANSMEM 17..38
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:D3Z338"
FT TOPO_DOM 39..51
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:D3Z338"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:D3Z338"
FT TOPO_DOM 73..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:D3Z338"
FT TRANSMEM 85..107
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:D3Z338"
FT TOPO_DOM 108..116
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:D3Z338"
FT CONFLICT 2
FT /note="W -> R (in Ref. 2; HY032040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 116 AA; 13758 MW; ACBDE16399DAD42C CRC64;
MWLQDRIATF FFPKGMMLTT AALMLFFLHL GIFIRDVHNF CITYHYDHMS FHYTVVLMFS
QVISICWAAM GSLYAEMTEN KYVCFSALTI LMLNGAMFFN RLSLEFLAIE YREEHH
