ID   KCNU1_HUMAN             Reviewed;        1149 AA.
AC   A8MYU2; B4DYE4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   02-SEP-2026, entry version 145.
DE   RecName: Full=Potassium channel subfamily U member 1;
DE   AltName: Full=Calcium-activated potassium channel subunit alpha-3;
DE   AltName: Full=Calcium-activated potassium channel, subfamily M subunit alpha-3;
DE   AltName: Full=KCa5;
DE   AltName: Full=Slowpoke homolog 3;
GN   Name=KCNU1 {ECO:0000312|HGNC:HGNC:18867};
GN   Synonyms=KCNMA3, KCNMC1, SLO3 {ECO:0000303|PubMed:9452476};
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], AND VARIANT SER-916.
RC   TISSUE=Testis;
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 GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [3]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=9452476; DOI=10.1074/jbc.273.6.3509;
RA   Schreiber M., Wei A., Yuan A., Gaut J., Saito M., Salkoff L.;
RT   "Slo3, a novel pH-sensitive K+ channel from mammalian spermatocytes.";
RL   J. Biol. Chem. 273:3509-3516(1998).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 330-1063, FUNCTION, TRANSPORTER
RP   ACTIVITY, SUBUNIT, AND ACTIVITY REGULATION.
RX   PubMed=23129643; DOI=10.1073/pnas.1215078109;
RA   Leonetti M.D., Yuan P., Hsiung Y., Mackinnon R.;
RT   "Functional and structural analysis of the human SLO3 pH- and voltage-gated
RT   K+ channel.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:19274-19279(2012).
RN   [5]
RP   FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=24670955; DOI=10.7554/elife.01438;
RA   Brenker C., Zhou Y., Mueller A., Echeverry F.A., Troetschel C., Poetsch A.,
RA   Xia X.M., Boenigk W., Lingle C.J., Kaupp U.B., Struenker T.;
RT   "The Ca2+-activated K+ current of human sperm is mediated by Slo3.";
RL   Elife 3:e01438-e01438(2014).
RN   [6]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=36649421; DOI=10.1073/pnas.2212338120;
RA   Lyon M., Li P., Ferreira J.J., Lazarenko R.M., Kharade S.V., Kramer M.,
RA   McClenahan S.J., Days E., Bauer J.A., Spitznagel B.D., Weaver C.D.,
RA   Borrego Alvarez A., Puga Molina L.C., Lybaert P., Khambekar S., Liu A.,
RA   Lindsley C.W., Denton J., Santi C.M.;
RT   "A selective inhibitor of the sperm-specific potassium channel SLO3 impairs
RT   human sperm function.";
RL   Proc. Natl. Acad. Sci. U.S.A. 120:e2212338120-e2212338120(2023).
RN   [7]
RP   FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX   PubMed=38267364; DOI=10.1093/biolre/ioae004;
RA   Zhang J., Zheng L., Chen Y., Luo T., Zeng X., Kang H.;
RT   "LRRC52 is likely a functional component of human KSper.";
RL   Biol. Reprod. 0:0-0(2024).
RN   [8]
RP   INVOLVEMENT IN SPGF79, VARIANT SPGF79 ARG-715, CHARACTERIZATION OF VARIANT
RP   SPGF79 ARG-715, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=35551387; DOI=10.1093/humrep/deac102;
RA   Liu R., Yan Z., Fan Y., Qu R., Chen B., Li B., Wu L., Wu H., Mu J.,
RA   Zhao L., Wang W., Dong J., Zeng Y., Li Q., Wang L., Sang Q., Zhang Z.,
RA   Kuang Y.;
RT   "Bi-allelic variants in KCNU1 cause impaired acrosome reactions and male
RT   infertility.";
RL   Hum. Reprod. 37:1394-1405(2022).
RN   [9]
RP   VARIANT SPGF79 PHE-413, CHARACTERIZATION OF VARIANT SPGF79 PHE-413,
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=34980136; DOI=10.1186/s12958-021-00880-4;
RA   Lv M., Liu C., Ma C., Yu H., Shao Z., Gao Y., Liu Y., Wu H., Tang D.,
RA   Tan Q., Zhang J., Li K., Xu C., Geng H., Zhang J., Li H., Mao X., Ge L.,
RA   Fu F., Zhong K., Xu Y., Tao F., Zhou P., Wei Z., He X., Zhang F., Cao Y.;
RT   "Homozygous mutation in SLO3 leads to severe asthenoteratozoospermia due to
RT   acrosome hypoplasia and mitochondrial sheath malformations.";
RL   Reprod. Biol. Endocrinol. 20:5-5(2022).
CC   -!- FUNCTION: Testis-specific potassium channel activated by both
CC       intracellular pH and membrane voltage that mediates export of K(+)
CC       (PubMed:23129643, PubMed:24670955, PubMed:36649421, PubMed:38267364,
CC       PubMed:9452476). Represents the primary spermatozoan K(+) current. The
CC       channel underlies a pH-triggered membrane hyperpolarization during the
CC       process of sperm capacitation, as sperm encounter the alkaline
CC       environment near the ovum in the female reproductive tract, thereby
CC       playing an essential for male fertility (PubMed:34980136,
CC       PubMed:35551387, PubMed:36649421). {ECO:0000269|PubMed:23129643,
CC       ECO:0000269|PubMed:24670955, ECO:0000269|PubMed:34980136,
CC       ECO:0000269|PubMed:35551387, ECO:0000269|PubMed:36649421,
CC       ECO:0000269|PubMed:38267364, ECO:0000269|PubMed:9452476}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000269|PubMed:23129643, ECO:0000269|PubMed:24670955};
CC   -!- ACTIVITY REGULATION: Regulated by changes in cytosolic pH; activated by
CC       alkalization (PubMed:23129643, PubMed:24670955). Activated by
CC       intracellular Ca(2+) (PubMed:24670955). Despite strong sequence
CC       similarity, human KCNU1 channels are significantly more sensitive to
CC       activation by internal Ca(2+) and less pH-sensitive than mouse KCNU1
CC       (PubMed:24670955). VU0546110 acts as a selective inhibitor
CC       (PubMed:36649421). The auxiliary subunit LRRC52 shifts the activation
CC       of KCNU1 to more negative potentials at a given pH (PubMed:38267364).
CC       {ECO:0000269|PubMed:23129643, ECO:0000269|PubMed:24670955,
CC       ECO:0000269|PubMed:36649421, ECO:0000269|PubMed:38267364}.
CC   -!- SUBUNIT: Homotetramer; which constitutes the activated potassium
CC       channel (By similarity). Interacts with LRRC52; this interaction
CC       changes channel gating properties, such as shifting gating to more
CC       negative potentials at a given pH (PubMed:38267364).
CC       {ECO:0000250|UniProtKB:Q12791, ECO:0000269|PubMed:38267364}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O54982};
CC       Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium,
CC       flagellum membrane {ECO:0000269|PubMed:24670955,
CC       ECO:0000269|PubMed:38267364}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:34980136,
CC       ECO:0000269|PubMed:35551387, ECO:0000269|PubMed:9452476}.
CC   -!- DOMAIN: The S4 segment, which is characterized by a series of
CC       positively charged amino acids at every third position, is part of the
CC       voltage-sensor. {ECO:0000250}.
CC   -!- DOMAIN: The pore-forming domain (also referred as P region) is imbedded
CC       into the membrane, and forms the selectivity filter of the pore. It
CC       contains the signature sequence of potassium channels that displays
CC       selectivity to potassium (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The RCK N-terminal domain mediates the homotetramerization,
CC       thereby promoting the assembly of monomers into functional potassium
CC       channel. {ECO:0000250|UniProtKB:Q12791}.
CC   -!- DOMAIN: The C-terminal cytosolic region confers the pH-dependence.
CC       {ECO:0000250}.
CC   -!- DISEASE: Spermatogenic failure 79 (SPGF79) [MIM:620196]: An autosomal
CC       recessive, male infertility disorder characterized by
CC       asthenoteratozoospermia with acrosome hypoplasia, disruption of the
CC       mitochondrial sheath, and reduced progressive sperm motility. The
CC       disorder is due to an abnormal acrosome reaction and impaired membrane
CC       potential after capacitation. {ECO:0000269|PubMed:34980136,
CC       ECO:0000269|PubMed:35551387}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the potassium channel family. Calcium-activated
CC       (TC 1.A.1.3) subfamily. KCa5.1/KCNU1 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AC124076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK302391; BAG63706.1; -; mRNA.
DR   CCDS; CCDS55220.1; -.
DR   RefSeq; NP_001027006.2; NM_001031836.3.
DR   PDB; 4HPF; X-ray; 3.40 A; A/B=330-1062.
DR   AlphaFoldDB; A8MYU2; -.
DR   SMR; A8MYU2; -.
DR   DIP; DIP-60091N; -.
DR   FunCoup; A8MYU2; 252.
DR   STRING; 9606.ENSP00000382770; -.
DR   ChEMBL; CHEMBL4524132; -.
DR   GuidetoPHARMACOLOGY; 387; -.
DR   GlyCosmos; A8MYU2; 1 site, 1 glycan.
DR   GlyGen; A8MYU2; 2 sites, 4 N-linked glycans (2 sites).
DR   iPTMnet; A8MYU2; -.
DR   PhosphoSitePlus; A8MYU2; -.
DR   BioMuta; KCNU1; -.
DR   MassIVE; A8MYU2; -.
DR   PaxDb; 9606-ENSP00000382770; -.
DR   PeptideAtlas; A8MYU2; -.
DR   ProteomicsDB; 2426; -.
DR   Antibodypedia; 57826; 75 antibodies from 13 providers.
DR   DNASU; 157855; -.
DR   Ensembl; ENST00000399881.8; ENSP00000382770.3; ENSG00000215262.8.
DR   GeneID; 157855; -.
DR   KEGG; hsa:157855; -.
DR   MANE-Select; ENST00000399881.8; ENSP00000382770.3; NM_001031836.3; NP_001027006.2.
DR   UCSC; uc010lvw.5; human.
DR   AGR; HGNC:18867; -.
DR   ClinPGx; PA38727; -.
DR   CTD; 157855; -.
DR   DisGeNET; 157855; -.
DR   GeneCards; KCNU1; -.
DR   HGNC; HGNC:18867; KCNU1.
DR   HPA; ENSG00000215262; Tissue enriched (testis).
DR   MalaCards; KCNU1; -.
DR   MIM; 615215; gene.
DR   MIM; 620196; phenotype.
DR   OpenTargets; ENSG00000215262; -.
DR   VEuPathDB; HostDB:ENSG00000215262; -.
DR   eggNOG; KOG1420; Eukaryota.
DR   GeneTree; ENSGT00940000161817; -.
DR   InParanoid; A8MYU2; -.
DR   OMA; NWNTGDN; -.
DR   OrthoDB; 10035564at2759; -.
DR   PAN-GO; A8MYU2; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; A8MYU2; -.
DR   PathwayCommons; A8MYU2; -.
DR   Reactome; R-HSA-1300642; Sperm Motility And Taxes.
DR   SignaLink; A8MYU2; -.
DR   Agora; ENSG00000215262; -.
DR   BioGRID-ORCS; 157855; 9 hits in 1147 CRISPR screens.
DR   ChiTaRS; KCNU1; human.
DR   EvolutionaryTrace; A8MYU2; -.
DR   GeneWiki; KCNU1; -.
DR   GenomeRNAi; 157855; -.
DR   Pharos; A8MYU2; Tbio.
DR   PRO; PR:A8MYU2; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; A8MYU2; protein.
DR   Bgee; ENSG00000215262; Expressed in sperm and 52 other cell types or tissues.
DR   ExpressionAtlas; A8MYU2; baseline and differential.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR   GO; GO:0005267; F:potassium channel activity; IMP:UniProtKB.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0022414; P:reproductive process; IMP:UniProtKB.
DR   FunFam; 3.40.50.720:FF:000005; calcium-activated potassium channel subunit alpha-1 isoform X6; 1.
DR   FunFam; 1.10.287.70:FF:000130; Potassium calcium-activated channel subfamily U member 1; 1.
DR   FunFam; 3.40.50.720:FF:000403; Potassium calcium-activated channel subfamily U member 1; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003929; K_chnl_BK_asu.
DR   InterPro; IPR047871; K_chnl_Slo-like.
DR   InterPro; IPR003148; RCK_N.
DR   InterPro; IPR048735; Slowpoke-like_C.
DR   PANTHER; PTHR10027; CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA CHAIN; 1.
DR   PANTHER; PTHR10027:SF23; POTASSIUM CHANNEL SUBFAMILY U MEMBER 1; 1.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF22614; Slo-like_RCK; 2.
DR   Pfam; PF21014; Slowpoke_C; 1.
DR   PRINTS; PR01449; BKCHANNELA.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   PROSITE; PS51201; RCK_N; 2.
DR   PDBsum; 4HPF; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cell projection; Cilium; Disease variant;
KW   Flagellum; Ion channel; Ion transport; Membrane; Potassium;
KW   Potassium channel; Potassium transport; Proteomics identification;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN           1..1149
FT                   /note="Potassium channel subfamily U member 1"
FT                   /id="PRO_0000349186"
FT   TOPO_DOM        1..24
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical; Name=Segment S0"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..101
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..138
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..188
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..226
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..247
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        248..259
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        260..282
FT                   /note="Pore-forming; Name=P region"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        283..291
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        313..1149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          331..473
FT                   /note="RCK N-terminal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT   DOMAIN          713..884
FT                   /note="RCK N-terminal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT   REGION          828..854
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1118..1149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           276..279
FT                   /note="Selectivity for potassium"
FT   COMPBIAS        830..840
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1125..1135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         175
FT                   /note="D -> N (in dbSNP:rs1111125)"
FT                   /id="VAR_060148"
FT   VARIANT         413
FT                   /note="I -> F (in SPGF79; severely decreased protein
FT                   abundance in patient sperm; dbSNP:rs377269265)"
FT                   /evidence="ECO:0000269|PubMed:34980136"
FT                   /id="VAR_088020"
FT   VARIANT         715
FT                   /note="H -> R (in SPGF79; no protein detected in patient
FT                   sperm; a knockin mouse model recapitulates the phenotype of
FT                   male infertility)"
FT                   /evidence="ECO:0000269|PubMed:35551387"
FT                   /id="VAR_088021"
FT   VARIANT         768
FT                   /note="W -> R (in dbSNP:rs28608091)"
FT                   /id="VAR_053868"
FT   VARIANT         916
FT                   /note="N -> S (in dbSNP:rs16885577)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_053869"
FT   CONFLICT        713
FT                   /note="R -> Q (in Ref. 1; BAG63706)"
FT                   /evidence="ECO:0000305"
FT   STRAND          333..338
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           342..349
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          363..365
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   TURN            382..385
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          386..388
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           397..403
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           405..407
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          408..413
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           422..439
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          445..448
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           452..456
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           457..460
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   TURN            466..469
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          471..473
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           475..488
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           492..498
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           512..521
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          527..529
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           532..534
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           539..549
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          553..558
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          571..573
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          585..591
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           593..597
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           598..600
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          685..690
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           697..700
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          716..720
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           732..735
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           736..739
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           745..747
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           748..750
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          751..755
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           757..763
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           764..767
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          771..778
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           783..788
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           791..793
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          795..800
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           801..804
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           815..825
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          861..864
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           868..870
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           871..878
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   TURN            882..884
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           889..891
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           893..897
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          899..901
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           903..907
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           909..915
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           917..928
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          962..966
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          968..971
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           972..975
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   HELIX           982..993
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          996..1003
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          1015..1020
FT                   /evidence="ECO:0007829|PDB:4HPF"
FT   STRAND          1032..1037
FT                   /evidence="ECO:0007829|PDB:4HPF"
SQ   SEQUENCE   1149 AA;  129543 MW;  BA527F41498B6AA7 CRC64;
     MFQTKLRNET WEDLPKMSCT TEIQAAFILS SFVTFFSGLI ILLIFRLIWR SVKKWQIIKG
     TGIILELFTS GTIARSHVRS LHFQGQFRDH IEMLLSAQTF VGQVLVILVF VLSIGSLIIY
     FINSADPVGS CSSYEDKTIP IDLVFNAFFS FYFGLRFMAA DDKIKFWLEM NSIVDIFTIP
     PTFISYYLKS NWLGLRFLRA LRLLELPQIL QILRAIKTSN SVKFSKLLSI ILSTWFTAAG
     FIHLVENSGD PWLKGRNSQN ISYFESIYLV MATTSTVGFG DVVAKTSLGR TFIMFFTLGS
     LILFANYIPE MVELFANKRK YTSSYEALKG KKFIVVCGNI TVDSVTAFLR NFLRDKSGEI
     NTEIVFLGET PPSLELETIF KCYLAYTTFI SGSAMKWEDL RRVAVESAEA CLIIANPLCS
     DSHAEDISNI MRVLSIKNYD STTRIIIQIL QSHNKVYLPK IPSWNWDTGD NIICFAELKL
     GFIAQGCLVP GLCTFLTSLF VEQNKKVMPK QTWKKHFLNS MKNKILTQRL SDDFAGMSFP
     EVARLCFLKM HLLLIAIEYK SLFTDGFCGL ILNPPPQVRI RKNTLGFFIA ETPKDVRRAL
     FYCSVCHDDV FIPELITNCG CKSRSRQHIT VPSVKRMKKC LKGISSRISG QDSPPRVSAS
     TSSISNFTTR TLQHDVEQDS DQLDSSGMFH WCKPTSLDKV TLKRTGKSKY KFRNHIVACV
     FGDAHSAPMG LRNFVMPLRA SNYTRKELKD IVFIGSLDYL QREWRFLWNF PQIYILPGCA
     LYSGDLHAAN IEQCSMCAVL SPPPQPSSNQ TLVDTEAIMA TLTIGSLQID SSSDPSPSVS
     EETPGYTNGH NEKSNCRKVP ILTELKNPSN IHFIEQLGGL EGSLQETNLH LSTAFSTGTV
     FSGSFLDSLL ATAFYNYHVL ELLQMLVTGG VSSQLEQHLD KDKVYGVADS CTSLLSGRNR
     CKLGLLSLHE TILSDVNPRN TFGQLFCGSL DLFGILCVGL YRIIDEEELN PENKRFVITR
     PANEFKLLPS DLVFCAIPFS TACYKRNEEF SLQKSYEIVN KASQTTETHS DTNCPPTIDS
     VTETLYSPVY SYQPRTNSLS FPKQIAWNQS RTNSIISSQI PLGDNAKENE RKTSDEVYDE
     DPFAYSEPL
//