SAHH3_HUMAN
ID SAHH3_HUMAN Reviewed; 611 AA.
AC Q96HN2; B4DIZ5; D9N155; O94917;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Adenosylhomocysteinase 3;
DE Short=AdoHcyase 3;
DE EC=3.3.1.1;
DE AltName: Full=IP(3)Rs binding protein released with IP(3) 2;
DE Short=IRBIT2;
DE AltName: Full=Long-IRBIT {ECO:0000303|PubMed:19220705};
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase 3;
DE AltName: Full=S-adenosylhomocysteine hydrolase-like protein 2;
GN Name=AHCYL2; Synonyms=KIAA0828;
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).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Colon mucosa, and Hippocampus;
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=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP FUNCTION, INTERACTION WITH AHCYL1, INTERACTION WITH ITPR1, AND
RP PHOSPHORYLATION AT SER-149; SER-152; SER-155 AND SER-158.
RX PubMed=19220705; DOI=10.1111/j.1471-4159.2009.05979.x;
RA Ando H., Mizutani A., Mikoshiba K.;
RT "An IRBIT homologue lacks binding activity to inositol 1,4,5-trisphosphate
RT receptor due to the unique N-terminal appendage.";
RL J. Neurochem. 109:539-550(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP INTERACTION WITH ZCCHC4.
RX PubMed=31799605; DOI=10.1093/nar/gkz1147;
RA Pinto R., Vaagboe C.B., Jakobsson M.E., Kim Y., Baltissen M.P.,
RA O'Donohue M.F., Guzman U.H., Malecki J.M., Wu J., Kirpekar F., Olsen J.V.,
RA Gleizes P.E., Vermeulen M., Leidel S.A., Slupphaug G., Falnes P.O.;
RT "The human methyltransferase ZCCHC4 catalyses N6-methyladenosine
RT modification of 28S ribosomal RNA.";
RL Nucleic Acids Res. 48:830-846(2020).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 175-607 IN COMPLEX WITH NAD, AND
RP SUBUNIT.
RG Structural genomics consortium (SGC);
RT "Human S-adenosyl homocysteine hydrolase-like 2 protein crystal
RT structure.";
RL Submitted (JUN-2009) to the PDB data bank.
CC -!- FUNCTION: May regulate the electrogenic sodium/bicarbonate
CC cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary
CC of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol
CC 1,4,5-trisphosphate (PubMed:19220705). {ECO:0000250|UniProtKB:A6QLP2,
CC ECO:0000269|PubMed:19220705}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.3.1.1;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Note=Binds 1 NAD(+) per subunit.;
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC -!- SUBUNIT: Homotetramer (Probable). Forms heteromultimers with AHCYL1
CC (via the C-terminal region) (PubMed:19220705). Interacts with ITPR1;
CC with lower affinity than AHCYL1 and maybe via ITPR1 (PubMed:19220705).
CC Interacts with SLC4A4 (By similarity). Interacts with ZCCHC4
CC (PubMed:31799605). {ECO:0000250|UniProtKB:A6QLP2,
CC ECO:0000269|PubMed:19220705, ECO:0000269|PubMed:31799605,
CC ECO:0000305|Ref.12}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A6QLP2,
CC ECO:0000250|UniProtKB:Q68FL4}. Microsome
CC {ECO:0000250|UniProtKB:Q68FL4}. Note=Associates with membranes when
CC phosphorylated, probably through interaction with ITPR1.
CC {ECO:0000250|UniProtKB:Q68FL4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96HN2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96HN2-2; Sequence=VSP_040095;
CC Name=3;
CC IsoId=Q96HN2-3; Sequence=VSP_043185, VSP_043186;
CC Name=4;
CC IsoId=Q96HN2-4; Sequence=VSP_046278, VSP_046279;
CC -!- PTM: Phosphorylated during neuronal differentiation at the LISN domain.
CC {ECO:0000250|UniProtKB:Q68FL4}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74851.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB020635; BAA74851.1; ALT_INIT; mRNA.
DR EMBL; AK025372; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK295851; BAG58657.1; -; mRNA.
DR EMBL; AK316073; BAH14444.1; -; mRNA.
DR EMBL; AC009244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC083866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008349; AAH08349.1; -; mRNA.
DR EMBL; BC024325; AAH24325.1; -; mRNA.
DR CCDS; CCDS47706.1; -. [Q96HN2-2]
DR CCDS; CCDS47707.2; -. [Q96HN2-3]
DR CCDS; CCDS47708.1; -. [Q96HN2-4]
DR CCDS; CCDS5812.1; -. [Q96HN2-1]
DR RefSeq; NP_001124192.1; NM_001130720.2. [Q96HN2-2]
DR RefSeq; NP_001124194.2; NM_001130722.2. [Q96HN2-3]
DR RefSeq; NP_001124195.1; NM_001130723.2. [Q96HN2-4]
DR RefSeq; NP_056143.1; NM_015328.3. [Q96HN2-1]
DR PDB; 3GVP; X-ray; 2.25 A; A/B/C/D=175-607.
DR PDBsum; 3GVP; -.
DR AlphaFoldDB; Q96HN2; -.
DR SMR; Q96HN2; -.
DR BioGRID; 116958; 138.
DR IntAct; Q96HN2; 68.
DR MINT; Q96HN2; -.
DR STRING; 9606.ENSP00000315931; -.
DR iPTMnet; Q96HN2; -.
DR PhosphoSitePlus; Q96HN2; -.
DR BioMuta; AHCYL2; -.
DR DMDM; 21759427; -.
DR EPD; Q96HN2; -.
DR jPOST; Q96HN2; -.
DR MassIVE; Q96HN2; -.
DR MaxQB; Q96HN2; -.
DR PaxDb; Q96HN2; -.
DR PeptideAtlas; Q96HN2; -.
DR PRIDE; Q96HN2; -.
DR ProteomicsDB; 15179; -.
DR ProteomicsDB; 76768; -. [Q96HN2-1]
DR ProteomicsDB; 76769; -. [Q96HN2-2]
DR ProteomicsDB; 76770; -. [Q96HN2-3]
DR Antibodypedia; 17876; 70 antibodies from 18 providers.
DR DNASU; 23382; -.
DR Ensembl; ENST00000325006.8; ENSP00000315931.3; ENSG00000158467.17. [Q96HN2-1]
DR Ensembl; ENST00000446544.6; ENSP00000413639.2; ENSG00000158467.17. [Q96HN2-2]
DR Ensembl; ENST00000474594.5; ENSP00000420459.1; ENSG00000158467.17. [Q96HN2-4]
DR Ensembl; ENST00000490911.5; ENSP00000420801.1; ENSG00000158467.17. [Q96HN2-3]
DR GeneID; 23382; -.
DR KEGG; hsa:23382; -.
DR MANE-Select; ENST00000325006.8; ENSP00000315931.3; NM_015328.4; NP_056143.1.
DR UCSC; uc003vot.4; human. [Q96HN2-1]
DR CTD; 23382; -.
DR DisGeNET; 23382; -.
DR GeneCards; AHCYL2; -.
DR HGNC; HGNC:22204; AHCYL2.
DR HPA; ENSG00000158467; Group enriched (choroid plexus, intestine).
DR MIM; 616520; gene.
DR neXtProt; NX_Q96HN2; -.
DR OpenTargets; ENSG00000158467; -.
DR PharmGKB; PA162376046; -.
DR VEuPathDB; HostDB:ENSG00000158467; -.
DR eggNOG; KOG1370; Eukaryota.
DR GeneTree; ENSGT00950000182981; -.
DR HOGENOM; CLU_025194_2_1_1; -.
DR InParanoid; Q96HN2; -.
DR OMA; QPTHLCE; -.
DR OrthoDB; 371693at2759; -.
DR PhylomeDB; Q96HN2; -.
DR TreeFam; TF300415; -.
DR PathwayCommons; Q96HN2; -.
DR Reactome; R-HSA-425381; Bicarbonate transporters.
DR SignaLink; Q96HN2; -.
DR SIGNOR; Q96HN2; -.
DR UniPathway; UPA00314; UER00076.
DR BioGRID-ORCS; 23382; 10 hits in 1074 CRISPR screens.
DR ChiTaRS; AHCYL2; human.
DR EvolutionaryTrace; Q96HN2; -.
DR GenomeRNAi; 23382; -.
DR Pharos; Q96HN2; Tbio.
DR PRO; PR:Q96HN2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96HN2; protein.
DR Bgee; ENSG00000158467; Expressed in rectum and 173 other tissues.
DR ExpressionAtlas; Q96HN2; baseline and differential.
DR Genevisible; Q96HN2; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; -; 3.
DR InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR InterPro; IPR000043; Adenosylhomocysteinase-like.
DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR PANTHER; PTHR23420; PTHR23420; 1.
DR Pfam; PF05221; AdoHcyase; 1.
DR Pfam; PF00670; AdoHcyase_NAD; 1.
DR SMART; SM00996; AdoHcyase; 1.
DR SMART; SM00997; AdoHcyase_NAD; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00936; ahcY; 1.
DR PROSITE; PS00738; ADOHCYASE_1; 1.
DR PROSITE; PS00739; ADOHCYASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Endoplasmic reticulum; Hydrolase; Microsome; NAD; One-carbon metabolism;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..611
FT /note="Adenosylhomocysteinase 3"
FT /id="PRO_0000116909"
FT REGION 1..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..109
FT /note="LISN domain, inhibits interaction with ITPR1"
FT /evidence="ECO:0000269|PubMed:19220705"
FT COMPBIAS 48..68
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 336..338
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 401..406
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.12"
FT BINDING 422
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.12"
FT BINDING 457
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.12"
FT BINDING 478..479
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.12"
FT BINDING 525
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.12"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19220705"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19220705"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19220705"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19220705"
FT VAR_SEQ 1..19
FT /note="MSVQVVSAAAAAKVPEVEL -> MEKWDGNEGTSAFHMPEWM (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046278"
FT VAR_SEQ 1..18
FT /note="MSVQVVSAAAAAKVPEVE -> MLGSKKKYIVNGNSGIKA (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043185"
FT VAR_SEQ 19..121
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043186"
FT VAR_SEQ 20..122
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046279"
FT VAR_SEQ 122
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10048485"
FT /id="VSP_040095"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:3GVP"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:3GVP"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 237..248
FT /evidence="ECO:0007829|PDB:3GVP"
FT STRAND 252..261
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 265..274
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 286..297
FT /evidence="ECO:0007829|PDB:3GVP"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 323..327
FT /evidence="ECO:0007829|PDB:3GVP"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 337..343
FT /evidence="ECO:0007829|PDB:3GVP"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 363..369
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 371..386
FT /evidence="ECO:0007829|PDB:3GVP"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 402..413
FT /evidence="ECO:0007829|PDB:3GVP"
FT STRAND 417..421
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 425..433
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:3GVP"
FT TURN 445..447
FT /evidence="ECO:0007829|PDB:3GVP"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 463..468
FT /evidence="ECO:0007829|PDB:3GVP"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:3GVP"
FT TURN 481..484
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 487..490
FT /evidence="ECO:0007829|PDB:3GVP"
FT STRAND 496..501
FT /evidence="ECO:0007829|PDB:3GVP"
FT STRAND 504..508
FT /evidence="ECO:0007829|PDB:3GVP"
FT STRAND 514..518
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 524..528
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 533..552
FT /evidence="ECO:0007829|PDB:3GVP"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:3GVP"
FT STRAND 560..564
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 567..577
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 578..581
FT /evidence="ECO:0007829|PDB:3GVP"
FT HELIX 590..596
FT /evidence="ECO:0007829|PDB:3GVP"
SQ SEQUENCE 611 AA; 66721 MW; A76B1275FC0D891D CRC64;
MSVQVVSAAA AAKVPEVELK DLSPSEAESQ LGLSTAAVGA MAPPAGGGDP EAPAPAAERP
PVPGPGSGPA AALSPAAGKV PQASAMKRSD PHHQHQRHRD GGEALVSPDG TVTEAPRTVK
KQIQFADQKQ EFNKRPTKIG RRSLSRSISQ SSTDSYSSAA SYTDSSDDET SPRDKQQKNS
KGSSDFCVKN IKQAEFGRRE IEIAEQEMPA LMALRKRAQG EKPLAGAKIV GCTHITAQTA
VLMETLGALG AQCRWAACNI YSTLNEVAAA LAESGFPVFA WKGESEDDFW WCIDRCVNVE
GWQPNMILDD GGDLTHWIYK KYPNMFKKIK GIVEESVTGV HRLYQLSKAG KLCVPAMNVN
DSVTKQKFDN LYCCRESILD GLKRTTDMMF GGKQVVVCGY GEVGKGCCAA LKAMGSIVYV
TEIDPICALQ ACMDGFRLVK LNEVIRQVDI VITCTGNKNV VTREHLDRMK NSCIVCNMGH
SNTEIDVASL RTPELTWERV RSQVDHVIWP DGKRIVLLAE GRLLNLSCST VPTFVLSITA
TTQALALIEL YNAPEGRYKQ DVYLLPKKMD EYVASLHLPT FDAHLTELTD EQAKYLGLNK
NGPFKPNYYR Y
