HDHD3_HUMAN
ID HDHD3_HUMAN Reviewed; 251 AA.
AC Q9BSH5; B2RD47;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein 3;
GN Name=HDHD3; Synonyms=C9orf158;
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].
RC TISSUE=Colon;
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=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-15, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 8-247.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human haloacid dehalogenase-like hydrolase domain
RT containing 3 (HDHD3).";
RL Submitted (NOV-2009) to the PDB data bank.
CC -!- INTERACTION:
CC Q9BSH5; Q7Z3C6-3: ATG9A; NbExp=3; IntAct=EBI-745201, EBI-12006308;
CC Q9BSH5; P33240: CSTF2; NbExp=3; IntAct=EBI-745201, EBI-711360;
CC Q9BSH5; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-745201, EBI-3867333;
CC Q9BSH5; Q9NW38: FANCL; NbExp=3; IntAct=EBI-745201, EBI-2339898;
CC Q9BSH5; O75593: FOXH1; NbExp=3; IntAct=EBI-745201, EBI-1759806;
CC Q9BSH5; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-745201, EBI-6426443;
CC Q9BSH5; Q9NRQ2: PLSCR4; NbExp=3; IntAct=EBI-745201, EBI-769257;
CC Q9BSH5; Q12837: POU4F2; NbExp=3; IntAct=EBI-745201, EBI-17236143;
CC Q9BSH5; O75360: PROP1; NbExp=3; IntAct=EBI-745201, EBI-9027467;
CC Q9BSH5; Q8NB12: SMYD1; NbExp=3; IntAct=EBI-745201, EBI-8463848;
CC Q9BSH5; Q08117-2: TLE5; NbExp=3; IntAct=EBI-745201, EBI-11741437;
CC Q9BSH5; Q15645: TRIP13; NbExp=6; IntAct=EBI-745201, EBI-358993;
CC Q9BSH5; Q08AM6: VAC14; NbExp=3; IntAct=EBI-745201, EBI-2107455;
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; AK315401; BAG37794.1; -; mRNA.
DR EMBL; AL137066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005048; AAH05048.1; -; mRNA.
DR EMBL; BC031878; AAH31878.1; -; mRNA.
DR CCDS; CCDS6793.1; -.
DR RefSeq; NP_001291438.1; NM_001304509.1.
DR RefSeq; NP_001291439.1; NM_001304510.1.
DR RefSeq; NP_001291440.1; NM_001304511.1.
DR RefSeq; NP_112496.1; NM_031219.3.
DR PDB; 3K1Z; X-ray; 1.55 A; A=8-247.
DR PDBsum; 3K1Z; -.
DR AlphaFoldDB; Q9BSH5; -.
DR SMR; Q9BSH5; -.
DR BioGRID; 123632; 56.
DR IntAct; Q9BSH5; 15.
DR STRING; 9606.ENSP00000238379; -.
DR DEPOD; HDHD3; -.
DR iPTMnet; Q9BSH5; -.
DR PhosphoSitePlus; Q9BSH5; -.
DR SwissPalm; Q9BSH5; -.
DR BioMuta; HDHD3; -.
DR DMDM; 74752302; -.
DR EPD; Q9BSH5; -.
DR jPOST; Q9BSH5; -.
DR MassIVE; Q9BSH5; -.
DR MaxQB; Q9BSH5; -.
DR PaxDb; Q9BSH5; -.
DR PeptideAtlas; Q9BSH5; -.
DR PRIDE; Q9BSH5; -.
DR ProteomicsDB; 78894; -.
DR Antibodypedia; 15302; 164 antibodies from 23 providers.
DR DNASU; 81932; -.
DR Ensembl; ENST00000238379.9; ENSP00000238379.5; ENSG00000119431.10.
DR Ensembl; ENST00000374180.4; ENSP00000363295.3; ENSG00000119431.10.
DR GeneID; 81932; -.
DR KEGG; hsa:81932; -.
DR MANE-Select; ENST00000374180.4; ENSP00000363295.3; NM_001304509.2; NP_001291438.1.
DR UCSC; uc004bhi.2; human.
DR CTD; 81932; -.
DR GeneCards; HDHD3; -.
DR HGNC; HGNC:28171; HDHD3.
DR HPA; ENSG00000119431; Tissue enhanced (adrenal).
DR neXtProt; NX_Q9BSH5; -.
DR OpenTargets; ENSG00000119431; -.
DR PharmGKB; PA134868152; -.
DR VEuPathDB; HostDB:ENSG00000119431; -.
DR eggNOG; KOG3085; Eukaryota.
DR GeneTree; ENSGT00390000015582; -.
DR HOGENOM; CLU_045011_8_0_1; -.
DR InParanoid; Q9BSH5; -.
DR OMA; CDYQGAR; -.
DR OrthoDB; 1119971at2759; -.
DR PhylomeDB; Q9BSH5; -.
DR TreeFam; TF315144; -.
DR PathwayCommons; Q9BSH5; -.
DR SignaLink; Q9BSH5; -.
DR BioGRID-ORCS; 81932; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; HDHD3; human.
DR EvolutionaryTrace; Q9BSH5; -.
DR GenomeRNAi; 81932; -.
DR Pharos; Q9BSH5; Tdark.
DR PRO; PR:Q9BSH5; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9BSH5; protein.
DR Bgee; ENSG00000119431; Expressed in right adrenal gland and 148 other tissues.
DR Genevisible; Q9BSH5; HS.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR Gene3D; 1.10.150.720; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR011949; HAD-SF_hydro_IA_REG-2-like.
DR InterPro; IPR044924; HAD-SF_hydro_IA_REG-2-like_cap.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02252; DREG-2; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Reference proteome.
FT CHAIN 1..251
FT /note="Haloacid dehalogenase-like hydrolase domain-
FT containing protein 3"
FT /id="PRO_0000287313"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 15
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CYW4"
FT VARIANT 146
FT /note="G -> E (in dbSNP:rs1043836)"
FT /id="VAR_032298"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:3K1Z"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:3K1Z"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 42..59
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 71..85
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:3K1Z"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:3K1Z"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:3K1Z"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3K1Z"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3K1Z"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:3K1Z"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:3K1Z"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:3K1Z"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:3K1Z"
SQ SEQUENCE 251 AA; 28000 MW; AFB5AF5C286A55DE CRC64;
MAHRLQIRLL TWDVKDTLLR LRHPLGEAYA TKARAHGLEV EPSALEQGFR QAYRAQSHSF
PNYGLSHGLT SRQWWLDVVL QTFHLAGVQD AQAVAPIAEQ LYKDFSHPCT WQVLDGAEDT
LRECRTRGLR LAVISNFDRR LEGILGGLGL REHFDFVLTS EAAGWPKPDP RIFQEALRLA
HMEPVVAAHV GDNYLCDYQG PRAVGMHSFL VVGPQALDPV VRDSVPKEHI LPSLAHLLPA
LDCLEGSTPG L
