ENO4_HUMAN
ID ENO4_HUMAN Reviewed; 625 AA.
AC A6NNW6; A0A087WZY6; A6NI74; B8ZZN9; J3KNX1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 4.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Enolase 4 {ECO:0000305};
DE EC=4.2.1.11 {ECO:0000250|UniProtKB:Q8C042};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
GN Name=ENO4 {ECO:0000312|HGNC:HGNC:31670}; Synonyms=C10orf134;
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).
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
CC -!- FUNCTION: May be required for sperm motility and function.
CC {ECO:0000250|UniProtKB:Q8C042}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11;
CC Evidence={ECO:0000250|UniProtKB:Q8C042};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000250|UniProtKB:Q8C042}.
CC -!- SUBUNIT: Interacts with ENO1 and AKAP4. {ECO:0000250|UniProtKB:Q8C042}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=A6NNW6-3; Sequence=Displayed;
CC Name=2;
CC IsoId=A6NNW6-2; Sequence=VSP_059947, VSP_059948;
CC Name=4;
CC IsoId=A6NNW6-4; Sequence=VSP_059949, VSP_059951, VSP_059950;
CC -!- PTM: Synthesized as an approximately 70-kDa precursor, which then
CC undergoes proteolytic cleavage to an approximately 60-kDa enzyme; HOATZ
CC associates directly or indirectly with ENO4 to mediate this process
CC before its transport to mature flagella.
CC {ECO:0000250|UniProtKB:Q8C042}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the enolase family, Leu-362 is present
CC instead of the conserved Glu which is expected to be an active site
CC residue. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX647301; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC023283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS73206.1; -. [A6NNW6-3]
DR RefSeq; NP_001229628.1; NM_001242699.1. [A6NNW6-3]
DR AlphaFoldDB; A6NNW6; -.
DR SMR; A6NNW6; -.
DR IntAct; A6NNW6; 3.
DR STRING; 9606.ENSP00000345555; -.
DR iPTMnet; A6NNW6; -.
DR PhosphoSitePlus; A6NNW6; -.
DR BioMuta; ENO4; -.
DR EPD; A6NNW6; -.
DR MassIVE; A6NNW6; -.
DR PaxDb; A6NNW6; -.
DR PeptideAtlas; A6NNW6; -.
DR PRIDE; A6NNW6; -.
DR ProteomicsDB; 1254; -.
DR ProteomicsDB; 1644; -. [A6NNW6-2]
DR Antibodypedia; 49029; 81 antibodies from 14 providers.
DR DNASU; 387712; -.
DR Ensembl; ENST00000341276.11; ENSP00000345555.6; ENSG00000188316.15. [A6NNW6-3]
DR Ensembl; ENST00000409522.5; ENSP00000387194.1; ENSG00000188316.15. [A6NNW6-2]
DR GeneID; 387712; -.
DR KEGG; hsa:387712; -.
DR MANE-Select; ENST00000341276.11; ENSP00000345555.6; NM_001242699.2; NP_001229628.1.
DR UCSC; uc001lcw.4; human. [A6NNW6-3]
DR UCSC; uc057wfb.1; human.
DR UCSC; uc057wfd.1; human.
DR CTD; 387712; -.
DR DisGeNET; 387712; -.
DR GeneCards; ENO4; -.
DR HGNC; HGNC:31670; ENO4.
DR HPA; ENSG00000188316; Tissue enhanced (brain, fallopian tube).
DR neXtProt; NX_A6NNW6; -.
DR OpenTargets; ENSG00000188316; -.
DR VEuPathDB; HostDB:ENSG00000188316; -.
DR eggNOG; KOG2670; Eukaryota.
DR GeneTree; ENSGT00950000182805; -.
DR HOGENOM; CLU_1079780_0_0_1; -.
DR InParanoid; A6NNW6; -.
DR OMA; LIIRHTN; -.
DR OrthoDB; 1097401at2759; -.
DR PhylomeDB; A6NNW6; -.
DR TreeFam; TF354238; -.
DR PathwayCommons; A6NNW6; -.
DR SignaLink; A6NNW6; -.
DR UniPathway; UPA00109; UER00187.
DR BioGRID-ORCS; 387712; 8 hits in 280 CRISPR screens.
DR ChiTaRS; ENO4; human.
DR GenomeRNAi; 387712; -.
DR Pharos; A6NNW6; Tbio.
DR PRO; PR:A6NNW6; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; A6NNW6; protein.
DR Bgee; ENSG00000188316; Expressed in right uterine tube and 86 other tissues.
DR ExpressionAtlas; A6NNW6; baseline and differential.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR GO; GO:0097228; C:sperm principal piece; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IBA:GO_Central.
DR GO; GO:0044782; P:cilium organization; IEA:Ensembl.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycolysis; Lyase; Reference proteome.
FT CHAIN 1..625
FT /note="Enolase 4"
FT /id="PRO_0000348454"
FT REGION 184..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..206
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 497
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 548
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..235
FT /note="Missing (in isoform 4)"
FT /id="VSP_059949"
FT VAR_SEQ 56..330
FT /note="Missing (in isoform 2)"
FT /id="VSP_059947"
FT VAR_SEQ 406..448
FT /note="NKGKYEVIMGTYKNAAEMVDLYVDLINKYPSIIALIDPFRKED -> D (in
FT isoform 2)"
FT /id="VSP_059948"
FT VAR_SEQ 575..598
FT /note="GFKEEHTFFYFNEEAEKAAEALEA -> ATSSSSCDARIGGQEQETMTLVKV
FT (in isoform 4)"
FT /id="VSP_059951"
FT VAR_SEQ 599..625
FT /note="Missing (in isoform 4)"
FT /id="VSP_059950"
FT CONFLICT 32
FT /note="V -> I (in Ref. 1; BX647301)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 68465 MW; 3FE6180EE2D83CE5 CRC64;
MEEEGGGRSC GTTRELQKLK QQAMEYYREN DVPRRLEELL NSTFYLQPAD VYGHLANCFS
KLAKPPTICK IVGKDVLDGL GLPTLQVDIF CTIQNFPKNV CSVVISTHFE VHENALPELA
KAEEAERASA VSTAVQWVNS TITHELQGMA PSDQAEVDHL LRIFFASKVQ EDKGRKELEK
SLEYSTVPTP LPPVPPPPPP PPPTKKKGQK PGRKDTITEK PIAPAEPVEP VLSGSMAIGA
VSLAVAKACA MLLNKPLYLN IALLKHNQEQ PTTLSMPLLM VSLVSCGKSS SGKLNLMKEV
ICIPHPELTT KQGVEMLMEM QKHINKIIEM PSPPKAETKK GHDGSKRGQQ QITGKMSHLG
CLTINCDSIE QPLLLIQEIC ANLGLELGTN LHLAINCAGH ELMDYNKGKY EVIMGTYKNA
AEMVDLYVDL INKYPSIIAL IDPFRKEDSE QWDSIYHALG SRCYIIAGTA SKSISKLLEQ
GNISIPKSNG LIIKHTNQTT MSDLVEITNL IDSKKHITVF GSTEGESSDD SLVDLAVGLG
VRFIKLGGLS RGERVTKYNR LLTIEEELVQ NGTLGFKEEH TFFYFNEEAE KAAEALEAAA
AREPLVPTFP TQGVEESAET GASSG
