EFCB9_HUMAN
ID EFCB9_HUMAN Reviewed; 197 AA.
AC A8MZ26;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=EF-hand calcium-binding domain-containing protein 9 {ECO:0000305};
GN Name=EFCAB9 {ECO:0000312|HGNC:HGNC:34530};
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=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
CC -!- FUNCTION: Auxiliary component of the CatSper complex, a complex
CC involved in sperm cell hyperactivation. pH-dependent Ca(2+) sensor
CC required to activate the CatSper channel. Sperm cell hyperactivation is
CC needed for sperm motility which is essential late in the preparation of
CC sperm for fertilization. Associates with the CatSper complex via direct
CC interaction with CATSPERZ, and senses intracellular Ca(2+). Together
CC with CATSPERZ, associates with the CatSper channel pore and is required
CC for the two-row structure of each single CatSper channel.
CC {ECO:0000250|UniProtKB:Q9DAM2}.
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 (By similarity). 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 (By similarity).
CC TMEM262/CATSPERH interacts with CATSPERB, further stabilizing the
CC complex. C2CD6/CATSPERT interacts at least with CATSPERD and is
CC required for targeting the CatSper complex in the flagellar membrane
CC (By similarity). Interacts with CATSPERZ; the interaction is direct,
CC Ca(2+)-dependent and connects EFCAB9 with the CatSper complex (By
CC similarity). Dissociates from CATSPERZ at elevated pH (By similarity).
CC {ECO:0000250|UniProtKB:Q91ZR5, ECO:0000250|UniProtKB:Q9DAM2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9DAM2}. Cell
CC projection, cilium, flagellum {ECO:0000250|UniProtKB:Q9DAM2}.
CC Note=Localizes to the principal piece of the sperm tail.
CC {ECO:0000250|UniProtKB:Q9DAM2}.
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; AC024561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS54946.1; -.
DR RefSeq; NP_001164654.1; NM_001171183.1.
DR AlphaFoldDB; A8MZ26; -.
DR SMR; A8MZ26; -.
DR STRING; 9606.ENSP00000381247; -.
DR TCDB; 1.A.1.19.1; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; A8MZ26; -.
DR PhosphoSitePlus; A8MZ26; -.
DR BioMuta; EFCAB9; -.
DR EPD; A8MZ26; -.
DR jPOST; A8MZ26; -.
DR MassIVE; A8MZ26; -.
DR PaxDb; A8MZ26; -.
DR PeptideAtlas; A8MZ26; -.
DR PRIDE; A8MZ26; -.
DR DNASU; 285588; -.
DR Ensembl; ENST00000398186.5; ENSP00000381247.4; ENSG00000214360.5.
DR GeneID; 285588; -.
DR KEGG; hsa:285588; -.
DR MANE-Select; ENST00000398186.5; ENSP00000381247.4; NM_001171183.2; NP_001164654.1.
DR UCSC; uc021yhr.2; human.
DR CTD; 285588; -.
DR DisGeNET; 285588; -.
DR GeneCards; EFCAB9; -.
DR HGNC; HGNC:34530; EFCAB9.
DR HPA; ENSG00000214360; Tissue enriched (testis).
DR MIM; 618520; gene.
DR neXtProt; NX_A8MZ26; -.
DR PharmGKB; PA164718963; -.
DR VEuPathDB; HostDB:ENSG00000214360; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00390000007501; -.
DR HOGENOM; CLU_106342_0_0_1; -.
DR InParanoid; A8MZ26; -.
DR OMA; EFYMLVC; -.
DR OrthoDB; 1306120at2759; -.
DR PhylomeDB; A8MZ26; -.
DR TreeFam; TF328944; -.
DR PathwayCommons; A8MZ26; -.
DR SignaLink; A8MZ26; -.
DR BioGRID-ORCS; 285588; 11 hits in 1058 CRISPR screens.
DR ChiTaRS; EFCAB9; human.
DR GenomeRNAi; 285588; -.
DR Pharos; A8MZ26; Tdark.
DR PRO; PR:A8MZ26; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; A8MZ26; protein.
DR Bgee; ENSG00000214360; Expressed in right testis and 34 other tissues.
DR GO; GO:0036128; C:CatSper complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0097228; C:sperm principal piece; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0061891; F:calcium ion sensor activity; 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; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR042798; EFCAB9.
DR PANTHER; PTHR47065; PTHR47065; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 3: Inferred from homology;
KW Calcium; Cell projection; Cilium; Cytoplasm; Flagellum; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..197
FT /note="EF-hand calcium-binding domain-containing protein 9"
FT /id="PRO_0000340648"
FT DOMAIN 59..94
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 100..135
FT /note="EF-hand 2"
FT /evidence="ECO:0000250|UniProtKB:Q9DAM2"
FT DOMAIN 136..171
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 177..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
SQ SEQUENCE 197 AA; 23937 MW; 248012FD9746D508 CRC64;
MRLKQGSFLW YLYLDKIYCL LSVRNVKALA EYFHILDVHG KNTLNDVLFY HFLHHVTDLK
KAQINIVFDM LDWNAVGEID FEKFYMLVCM LLAHQNHLEG QFMYRHSRPV FDLLDLKGDL
RIGAKNFEMY RFLFNIQKQE LKDLFRDFDI TGDNRLNYQE FKLYTIIYTD KLQKRQKTEE
KEKGERKRSL YSKCHIK
