HAGHL_HUMAN
ID HAGHL_HUMAN Reviewed; 290 AA.
AC Q6PII5; A6NCC4; D3DU64; Q59FX8; Q96BZ3; Q96NR5; Q96S11; Q9BT45;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Hydroxyacylglutathione hydrolase-like protein;
DE EC=3.1.2.-;
GN Name=HAGHL;
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 3).
RC TISSUE=Cerebellum;
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=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Brain, Eye, and Skin;
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-191.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolase acting on ester bonds. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC Q6PII5; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-6255752, EBI-10226858;
CC Q6PII5; D3DTS7: PMP22; NbExp=3; IntAct=EBI-6255752, EBI-25882629;
CC Q6PII5; Q8NE91: TM4SF1; NbExp=3; IntAct=EBI-6255752, EBI-25875545;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6PII5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PII5-2; Sequence=VSP_030054;
CC Name=3;
CC IsoId=Q6PII5-3; Sequence=VSP_030053, VSP_030055;
CC Name=4;
CC IsoId=Q6PII5-4; Sequence=VSP_030052, VSP_030056;
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK61250.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD92568.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD92568.1; Type=Miscellaneous discrepancy; Note=Sequence of unknown origin at the C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK054841; BAB70814.1; -; mRNA.
DR EMBL; AE006464; AAK61250.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z98258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85726.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85730.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85731.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85732.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85733.1; -; Genomic_DNA.
DR EMBL; BC004353; AAH04353.1; -; mRNA.
DR EMBL; BC015008; AAH15008.1; -; mRNA.
DR EMBL; BC033796; AAH33796.1; -; mRNA.
DR EMBL; AB209331; BAD92568.1; ALT_SEQ; mRNA.
DR CCDS; CCDS32354.1; -. [Q6PII5-2]
DR RefSeq; NP_001277066.1; NM_001290137.1. [Q6PII5-2]
DR RefSeq; NP_001277068.1; NM_001290139.1. [Q6PII5-2]
DR RefSeq; NP_001310564.1; NM_001323635.1. [Q6PII5-2]
DR RefSeq; NP_115680.1; NM_032304.3. [Q6PII5-2]
DR RefSeq; XP_005255688.1; XM_005255631.4. [Q6PII5-1]
DR RefSeq; XP_011521013.1; XM_011522711.1.
DR RefSeq; XP_016879262.1; XM_017023773.1.
DR AlphaFoldDB; Q6PII5; -.
DR SMR; Q6PII5; -.
DR BioGRID; 123991; 4.
DR IntAct; Q6PII5; 6.
DR MINT; Q6PII5; -.
DR STRING; 9606.ENSP00000374353; -.
DR iPTMnet; Q6PII5; -.
DR PhosphoSitePlus; Q6PII5; -.
DR BioMuta; HAGHL; -.
DR DMDM; 74737738; -.
DR EPD; Q6PII5; -.
DR jPOST; Q6PII5; -.
DR MassIVE; Q6PII5; -.
DR MaxQB; Q6PII5; -.
DR PaxDb; Q6PII5; -.
DR PeptideAtlas; Q6PII5; -.
DR PRIDE; Q6PII5; -.
DR ProteomicsDB; 67158; -. [Q6PII5-1]
DR ProteomicsDB; 67159; -. [Q6PII5-2]
DR ProteomicsDB; 67160; -. [Q6PII5-3]
DR ProteomicsDB; 67161; -. [Q6PII5-4]
DR Antibodypedia; 59077; 165 antibodies from 13 providers.
DR DNASU; 84264; -.
DR Ensembl; ENST00000341413.8; ENSP00000341952.4; ENSG00000103253.19. [Q6PII5-1]
DR Ensembl; ENST00000389703.8; ENSP00000374353.3; ENSG00000103253.19. [Q6PII5-2]
DR Ensembl; ENST00000549114.5; ENSP00000447170.1; ENSG00000103253.19. [Q6PII5-3]
DR Ensembl; ENST00000564537.5; ENSP00000457219.1; ENSG00000103253.19. [Q6PII5-3]
DR GeneID; 84264; -.
DR KEGG; hsa:84264; -.
DR MANE-Select; ENST00000389703.8; ENSP00000374353.3; NM_032304.4; NP_115680.1. [Q6PII5-2]
DR UCSC; uc002cjl.1; human. [Q6PII5-1]
DR CTD; 84264; -.
DR DisGeNET; 84264; -.
DR GeneCards; HAGHL; -.
DR HGNC; HGNC:14177; HAGHL.
DR HPA; ENSG00000103253; Low tissue specificity.
DR neXtProt; NX_Q6PII5; -.
DR OpenTargets; ENSG00000103253; -.
DR PharmGKB; PA29180; -.
DR VEuPathDB; HostDB:ENSG00000103253; -.
DR eggNOG; KOG0813; Eukaryota.
DR GeneTree; ENSGT00940000161924; -.
DR HOGENOM; CLU_030571_4_4_1; -.
DR InParanoid; Q6PII5; -.
DR OMA; CKERARF; -.
DR OrthoDB; 961826at2759; -.
DR PhylomeDB; Q6PII5; -.
DR TreeFam; TF105273; -.
DR PathwayCommons; Q6PII5; -.
DR SignaLink; Q6PII5; -.
DR BioGRID-ORCS; 84264; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; HAGHL; human.
DR GenomeRNAi; 84264; -.
DR Pharos; Q6PII5; Tdark.
DR PRO; PR:Q6PII5; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6PII5; protein.
DR Bgee; ENSG00000103253; Expressed in pancreatic ductal cell and 156 other tissues.
DR ExpressionAtlas; Q6PII5; baseline and differential.
DR Genevisible; Q6PII5; HS.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR035680; Clx_II_MBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..290
FT /note="Hydroxyacylglutathione hydrolase-like protein"
FT /id="PRO_0000313601"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 97..203
FT /note="FGAIHVRCLLTPGHTAGHMSYFLWEDDCPDPPALFSGDALSVAGCGSCLEGS
FT AQQMYQSLAELGTLPPETKVFCGHEHTLSNLEFAQKVEPCNDHVRAKLSWAKARP ->
FT VSARSREGRGGRPGSTRPHRSACSSAAVRGHPRALPPDARPHRRPHELLPVGGRLPGPT
FT RPVLGRRAVGGRLRLVPGGQRPADVPEPGRAGYPAPRDEGVLRPRAHA (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030052"
FT VAR_SEQ 134..202
FT /note="DALSVAGCGSCLEGSAQQMYQSLAELGTLPPETKVFCGHEHTLSNLEFAQKV
FT EPCNDHVRAKLSWAKAR -> TRSAERAHPASRRPRPICSDPPSPARRRAVGGRLRLVP
FT GGQRPADVPEPGRAGYPAPRDEGVLRPRAHA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030053"
FT VAR_SEQ 201..290
FT /note="ARPLSRRGKRVGGEGTGFGVGGALRQGLMVTGACGHSRRGMRMTCPLCRRLW
FT ARSASTTPSCGWREYGCCPGASTVTWTLRKASGDCVLG -> KRDEDDVPTVPSTLGEE
FT RLYNPFLRVAEEPVRKFTGKAVPADVLEALCKERARFEQAGEPRQPQARALLALQWGLL
FT SAAPHD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030054"
FT VAR_SEQ 203..290
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030055"
FT VAR_SEQ 204..290
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030056"
SQ SEQUENCE 290 AA; 31557 MW; C0B2D01D53262AB2 CRC64;
MKVKVIPVLE DNYMYLVIEE LTREAVAVDV AVPKRLLEIV GREGVSLTAV LTTHHHWDHA
RGNPELARLR PGLAVLGADE RIFSLTRRLA HGEELRFGAI HVRCLLTPGH TAGHMSYFLW
EDDCPDPPAL FSGDALSVAG CGSCLEGSAQ QMYQSLAELG TLPPETKVFC GHEHTLSNLE
FAQKVEPCND HVRAKLSWAK ARPLSRRGKR VGGEGTGFGV GGALRQGLMV TGACGHSRRG
MRMTCPLCRR LWARSASTTP SCGWREYGCC PGASTVTWTL RKASGDCVLG
