A16A1_HUMAN
ID A16A1_HUMAN Reviewed; 802 AA.
AC Q8IZ83; B4DLQ1; C9JBH6; Q86YF0; Q8IYL4; Q8TEI8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Aldehyde dehydrogenase family 16 member A1;
GN Name=ALDH16A1;
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), AND VARIANT VAL-227.
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-227.
RC TISSUE=Lymph, Skin, and Uterus;
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 [5]
RP INTERACTION WITH SPG21.
RX PubMed=19184135; DOI=10.1007/s10048-009-0172-6;
RA Hanna M.C., Blackstone C.;
RT "Interaction of the SPG21 protein ACP33/maspardin with the aldehyde
RT dehydrogenase ALDH16A1.";
RL Neurogenetics 10:217-228(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
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 [8]
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 -!- SUBUNIT: Interacts with SPG21. {ECO:0000269|PubMed:19184135}.
CC -!- INTERACTION:
CC Q8IZ83; Q9Y315: DERA; NbExp=6; IntAct=EBI-1044483, EBI-1048152;
CC Q8IZ83; Q9Y2H0-1: DLGAP4; NbExp=3; IntAct=EBI-1044483, EBI-12000556;
CC Q8IZ83; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-1044483, EBI-22310682;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IZ83-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZ83-2; Sequence=VSP_029982, VSP_029983;
CC Name=3;
CC IsoId=Q8IZ83-3; Sequence=VSP_043280;
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- CAUTION: The active site cysteine and glutamate residues are not
CC conserved in this protein. Its activity is therefore unsure.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH35641.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB84962.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AK074136; BAB84962.1; ALT_SEQ; mRNA.
DR EMBL; AK297101; BAG59613.1; -; mRNA.
DR EMBL; AC010619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014895; AAH14895.2; -; mRNA.
DR EMBL; BC035641; AAH35641.1; ALT_INIT; mRNA.
DR EMBL; BC042142; AAH42142.1; -; mRNA.
DR CCDS; CCDS12766.1; -. [Q8IZ83-1]
DR CCDS; CCDS46141.1; -. [Q8IZ83-3]
DR RefSeq; NP_001138868.1; NM_001145396.1. [Q8IZ83-3]
DR RefSeq; NP_699160.2; NM_153329.3. [Q8IZ83-1]
DR AlphaFoldDB; Q8IZ83; -.
DR SASBDB; Q8IZ83; -.
DR SMR; Q8IZ83; -.
DR BioGRID; 125959; 48.
DR IntAct; Q8IZ83; 21.
DR MINT; Q8IZ83; -.
DR STRING; 9606.ENSP00000293350; -.
DR ChEMBL; CHEMBL4295896; -.
DR GlyGen; Q8IZ83; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q8IZ83; -.
DR MetOSite; Q8IZ83; -.
DR PhosphoSitePlus; Q8IZ83; -.
DR BioMuta; ALDH16A1; -.
DR DMDM; 269849532; -.
DR EPD; Q8IZ83; -.
DR jPOST; Q8IZ83; -.
DR MassIVE; Q8IZ83; -.
DR MaxQB; Q8IZ83; -.
DR PaxDb; Q8IZ83; -.
DR PeptideAtlas; Q8IZ83; -.
DR PRIDE; Q8IZ83; -.
DR ProteomicsDB; 71287; -. [Q8IZ83-1]
DR ProteomicsDB; 71288; -. [Q8IZ83-2]
DR ProteomicsDB; 71289; -. [Q8IZ83-3]
DR Antibodypedia; 32011; 101 antibodies from 18 providers.
DR DNASU; 126133; -.
DR Ensembl; ENST00000293350.9; ENSP00000293350.3; ENSG00000161618.10. [Q8IZ83-1]
DR Ensembl; ENST00000455361.6; ENSP00000410142.1; ENSG00000161618.10. [Q8IZ83-3]
DR GeneID; 126133; -.
DR KEGG; hsa:126133; -.
DR MANE-Select; ENST00000293350.9; ENSP00000293350.3; NM_153329.4; NP_699160.2.
DR UCSC; uc002pnt.4; human. [Q8IZ83-1]
DR CTD; 126133; -.
DR DisGeNET; 126133; -.
DR GeneCards; ALDH16A1; -.
DR HGNC; HGNC:28114; ALDH16A1.
DR HPA; ENSG00000161618; Low tissue specificity.
DR MIM; 613358; gene.
DR neXtProt; NX_Q8IZ83; -.
DR OpenTargets; ENSG00000161618; -.
DR PharmGKB; PA134903503; -.
DR VEuPathDB; HostDB:ENSG00000161618; -.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000161135; -.
DR HOGENOM; CLU_018339_0_0_1; -.
DR InParanoid; Q8IZ83; -.
DR OMA; MDYGPAP; -.
DR OrthoDB; 1070579at2759; -.
DR PhylomeDB; Q8IZ83; -.
DR TreeFam; TF329461; -.
DR PathwayCommons; Q8IZ83; -.
DR SignaLink; Q8IZ83; -.
DR BioGRID-ORCS; 126133; 13 hits in 1081 CRISPR screens.
DR ChiTaRS; ALDH16A1; human.
DR GeneWiki; ALDH16A1; -.
DR GenomeRNAi; 126133; -.
DR Pharos; Q8IZ83; Tdark.
DR PRO; PR:Q8IZ83; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8IZ83; protein.
DR Bgee; ENSG00000161618; Expressed in granulocyte and 141 other tissues.
DR ExpressionAtlas; Q8IZ83; baseline and differential.
DR Genevisible; Q8IZ83; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 2.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR011408; Aldehyde_DH.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699:SF211; PTHR11699:SF211; 2.
DR Pfam; PF00171; Aldedh; 2.
DR PIRSF; PIRSF036490; Aldedh_dupl; 1.
DR SUPFAM; SSF53720; SSF53720; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Reference proteome.
FT CHAIN 1..802
FT /note="Aldehyde dehydrogenase family 16 member A1"
FT /id="PRO_0000312986"
FT VAR_SEQ 254..308
FT /note="EGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGPG
FT GLR -> VPSGQGSWRNAAGGRKAPPAAELGGVPRKGVPFDGAWRESVRSWAWRWGRSR
FT CCC (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_029982"
FT VAR_SEQ 254..304
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043280"
FT VAR_SEQ 309..802
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_029983"
FT VARIANT 110
FT /note="E -> K (in dbSNP:rs3745312)"
FT /id="VAR_037638"
FT VARIANT 227
FT /note="L -> V (in dbSNP:rs1320303)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_037639"
SQ SEQUENCE 802 AA; 85127 MW; 2820628CD0EF5823 CRC64;
MAATRAGPRA REIFTSLEYG PVPESHACAL AWLDTQDRCL GHYVNGKWLK PEHRNSVPCQ
DPITGENLAS CLQAQAEDVA AAVEAARMAF KGWSAHPGVV RAQHLTRLAE VIQKHQRLLW
TLESLVTGRA VREVRDGDVQ LAQQLLHYHA IQASTQEEAL AGWEPMGVIG LILPPTFSFL
EMMWRICPAL AVGCTVVALV PPASPAPLLL AQLAGELGPF PGILNVLSGP ASLVPILASQ
PGIRKVAFCG APEEGRALRR SLAGECAELG LALGTESLLL LTDTADVDSA VEGVVDAAWS
DRGPGGLRLL IQESVWDEAM RRLQERMGRL RSGRGLDGAV DMGARGAAAC DLVQRFVREA
QSQGAQVFQA GDVPSERPFY PPTLVSNLPP ASPCAQVEVP WPVVVASPFR TAKEALLVAN
GTPRGGSASV WSERLGQALE LGYGLQVGTV WINAHGLRDP SVPTGGCKES GCSWHGGPDG
LYEYLRPSGT PARLSCLSKN LNYDTFGLAV PSTLPAGPEI GPSPAPPYGL FVGGRFQAPG
ARSSRPIRDS SGNLHGYVAE GGAKDIRGAV EAAHQAFPGW AGQSPGARAA LLWALAAALE
RRKSTLASRL ERQGAELKAA EAEVELSARR LRAWGARVQA QGHTLQVAGL RGPVLRLREP
LGVLAVVCPD EWPLLAFVSL LAPALAYGNT VVMVPSAACP LLALEVCQDM ATVFPAGLAN
VVTGDRDHLT RCLALHQDVQ AMWYFGSAQG SQFVEWASAG NLKPVWASRG CPRAWDQEAE
GAGPELGLRV ARTKALWLPM GD
