AB17B_HUMAN
ID AB17B_HUMAN Reviewed; 288 AA.
AC Q5VST6; A8KAJ5; Q5VST7; Q86YB6; Q8IY03; Q9Y377;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Alpha/beta hydrolase domain-containing protein 17B {ECO:0000305};
DE Short=Abhydrolase domain-containing protein 17B {ECO:0000312|HGNC:HGNC:24278};
DE EC=3.1.2.22 {ECO:0000269|PubMed:26701913};
GN Name=ABHD17B {ECO:0000312|HGNC:HGNC:24278}; Synonyms=C9orf77, FAM108B1;
GN ORFNames=CGI-67;
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=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-169.
RC TISSUE=Brain, 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 FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=26701913; DOI=10.7554/elife.11306;
RA Lin D.T., Conibear E.;
RT "ABHD17 proteins are novel protein depalmitoylases that regulate N-Ras
RT palmitate turnover and subcellular localization.";
RL Elife 4:E11306-E11306(2015).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in
CC proteins (PubMed:26701913). Has depalmitoylating activity towards
CC DLG4/PSD95 (PubMed:26701913). Has depalmitoylating activity towards
CC GAP43 (By similarity). Has depalmitoylating activity towards MAP6 (By
CC similarity). Has depalmitoylating activity towards NRAS
CC (PubMed:26701913). {ECO:0000250|UniProtKB:Q7M759,
CC ECO:0000269|PubMed:26701913}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:74151; EC=3.1.2.22;
CC Evidence={ECO:0000269|PubMed:26701913};
CC -!- ACTIVITY REGULATION: Inhibited by palmostatin-B.
CC {ECO:0000269|PubMed:26701913}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7M759};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q7M759}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q7M759}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q7M759}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q7M759}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q7M759}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q7M759}. Postsynaptic density membrane
CC {ECO:0000250|UniProtKB:Q7M759}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VST6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VST6-2; Sequence=VSP_023975;
CC -!- PTM: Palmitoylated on cysteine residues located in a cysteine cluster
CC at the N-terminus which promotes membrane localization. Palmitoylation
CC is required for post-synaptic localization and for depalmitoylating
CC activity towards DLG4/PSD95. {ECO:0000250|UniProtKB:Q7M759}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD17 family.
CC {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; AF151825; AAD34062.1; -; mRNA.
DR EMBL; AK293060; BAF85749.1; -; mRNA.
DR EMBL; AL138751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62521.1; -; Genomic_DNA.
DR EMBL; BC038390; AAH38390.2; -; mRNA.
DR EMBL; BC044576; AAH44576.1; -; mRNA.
DR CCDS; CCDS35042.1; -. [Q5VST6-2]
DR CCDS; CCDS35043.1; -. [Q5VST6-1]
DR RefSeq; NP_001020951.1; NM_001025780.2. [Q5VST6-1]
DR RefSeq; NP_057098.2; NM_016014.3. [Q5VST6-2]
DR RefSeq; XP_006717197.2; XM_006717134.3. [Q5VST6-2]
DR RefSeq; XP_016870276.1; XM_017014787.1. [Q5VST6-2]
DR RefSeq; XP_016870277.1; XM_017014788.1. [Q5VST6-1]
DR RefSeq; XP_016870278.1; XM_017014789.1. [Q5VST6-1]
DR AlphaFoldDB; Q5VST6; -.
DR SMR; Q5VST6; -.
DR BioGRID; 119293; 61.
DR IntAct; Q5VST6; 18.
DR STRING; 9606.ENSP00000366240; -.
DR ChEMBL; CHEMBL2189132; -.
DR ESTHER; human-ABHD17B; ABHD17-depalmitoylase.
DR MEROPS; S09.055; -.
DR iPTMnet; Q5VST6; -.
DR PhosphoSitePlus; Q5VST6; -.
DR SwissPalm; Q5VST6; -.
DR BioMuta; ABHD17B; -.
DR DMDM; 74746845; -.
DR EPD; Q5VST6; -.
DR jPOST; Q5VST6; -.
DR MassIVE; Q5VST6; -.
DR MaxQB; Q5VST6; -.
DR PaxDb; Q5VST6; -.
DR PeptideAtlas; Q5VST6; -.
DR PRIDE; Q5VST6; -.
DR ProteomicsDB; 65278; -. [Q5VST6-1]
DR ProteomicsDB; 65279; -. [Q5VST6-2]
DR Antibodypedia; 26944; 33 antibodies from 15 providers.
DR DNASU; 51104; -.
DR Ensembl; ENST00000333421.7; ENSP00000330222.6; ENSG00000107362.14. [Q5VST6-1]
DR Ensembl; ENST00000377041.6; ENSP00000366240.2; ENSG00000107362.14. [Q5VST6-2]
DR GeneID; 51104; -.
DR KEGG; hsa:51104; -.
DR MANE-Select; ENST00000333421.7; ENSP00000330222.6; NM_001025780.3; NP_001020951.1.
DR UCSC; uc004ail.4; human. [Q5VST6-1]
DR CTD; 51104; -.
DR GeneCards; ABHD17B; -.
DR HGNC; HGNC:24278; ABHD17B.
DR HPA; ENSG00000107362; Low tissue specificity.
DR MIM; 617943; gene.
DR neXtProt; NX_Q5VST6; -.
DR OpenTargets; ENSG00000107362; -.
DR PharmGKB; PA162385624; -.
DR VEuPathDB; HostDB:ENSG00000107362; -.
DR eggNOG; KOG1552; Eukaryota.
DR GeneTree; ENSGT00940000157611; -.
DR HOGENOM; CLU_029375_5_4_1; -.
DR InParanoid; Q5VST6; -.
DR OMA; FMTRTCK; -.
DR OrthoDB; 691954at2759; -.
DR PhylomeDB; Q5VST6; -.
DR TreeFam; TF314365; -.
DR PathwayCommons; Q5VST6; -.
DR Reactome; R-HSA-9648002; RAS processing.
DR SignaLink; Q5VST6; -.
DR BioGRID-ORCS; 51104; 18 hits in 1076 CRISPR screens.
DR ChiTaRS; ABHD17B; human.
DR GenomeRNAi; 51104; -.
DR Pharos; Q5VST6; Tbio.
DR PRO; PR:Q5VST6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5VST6; protein.
DR Bgee; ENSG00000107362; Expressed in endothelial cell and 181 other tissues.
DR ExpressionAtlas; Q5VST6; baseline and differential.
DR Genevisible; Q5VST6; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IMP:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:1902817; P:negative regulation of protein localization to microtubule; IEA:Ensembl.
DR GO; GO:1905668; P:positive regulation of protein localization to endosome; IEA:Ensembl.
DR GO; GO:0002084; P:protein depalmitoylation; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:1902950; P:regulation of dendritic spine maintenance; IEA:Ensembl.
DR GO; GO:0099175; P:regulation of postsynapse organization; IBA:GO_Central.
DR GO; GO:1902473; P:regulation of protein localization to synapse; IEA:Ensembl.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Endosome; Hydrolase;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Synapse.
FT CHAIN 1..288
FT /note="Alpha/beta hydrolase domain-containing protein 17B"
FT /id="PRO_0000281111"
FT ACT_SITE 170
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q96GS6"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M759"
FT VAR_SEQ 287..288
FT /note="NL -> QKHKEGK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10810093"
FT /id="VSP_023975"
FT VARIANT 154
FT /note="R -> K (in dbSNP:rs12380380)"
FT /id="VAR_054080"
FT VARIANT 169
FT /note="Q -> K (in dbSNP:rs17854317)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031230"
FT CONFLICT 18..21
FT /note="CPGK -> LSGE (in Ref. 1; AAD34062)"
FT /evidence="ECO:0000305"
FT CONFLICT 43..44
FT /note="GS -> RT (in Ref. 1; AAD34062)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="K -> E (in Ref. 1; AAD34062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 32215 MW; F315AF711AF532BD CRC64;
MNNLSFSELC CLFCCPPCPG KIASKLAFLP PDPTYTLMCD ESGSRWTLHL SERADWQYSS
REKDAIECFM TRTSKGNRIA CMFVRCSPNA KYTLLFSHGN AVDLGQMSSF YIGLGSRINC
NIFSYDYSGY GASSGKPTEK NLYADIEAAW LALRTRYGIR PENVIIYGQS IGTVPSVDLA
ARYESAAVIL HSPLTSGMRV AFPDTKKTYC FDAFPNIDKI SKITSPVLII HGTEDEVIDF
SHGLALFERC QRPVEPLWVE GAGHNDVELY GQYLERLKQF VSQELVNL
