ID   1A1L2_HUMAN             Reviewed;         568 AA.
AC   Q4AC99;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   24-JAN-2024, entry version 127.
DE   RecName: Full=Probable inactive 1-aminocyclopropane-1-carboxylate synthase-like protein 2;
DE            Short=ACC synthase-like protein 2;
GN   Name=ACCSL;
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], AND VARIANT ARG-529.
RA   Totoki Y., Yada T., Sakaki Y., Takeda T.;
RT   "Identification of novel human genes predicted by combining multiple gene-
RT   finders.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
CC   -!- CAUTION: While belonging to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family, it lacks a number of residues which are
CC       necessary for activity thus suggesting that it lacks enzymatic
CC       activity. {ECO:0000305}.
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DR   EMBL; AB231734; BAE17132.1; -; mRNA.
DR   EMBL; AC134775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS41636.1; -.
DR   RefSeq; NP_001027025.2; NM_001031854.2.
DR   AlphaFoldDB; Q4AC99; -.
DR   SMR; Q4AC99; -.
DR   BioGRID; 133403; 1.
DR   STRING; 9606.ENSP00000368109; -.
DR   iPTMnet; Q4AC99; -.
DR   PhosphoSitePlus; Q4AC99; -.
DR   BioMuta; ACCSL; -.
DR   DMDM; 296439453; -.
DR   MassIVE; Q4AC99; -.
DR   PaxDb; 9606-ENSP00000368109; -.
DR   PeptideAtlas; Q4AC99; -.
DR   Antibodypedia; 26088; 52 antibodies from 17 providers.
DR   DNASU; 390110; -.
DR   Ensembl; ENST00000378832.1; ENSP00000368109.1; ENSG00000205126.2.
DR   GeneID; 390110; -.
DR   KEGG; hsa:390110; -.
DR   MANE-Select; ENST00000378832.1; ENSP00000368109.1; NM_001031854.2; NP_001027025.2.
DR   UCSC; uc001mxw.1; human.
DR   AGR; HGNC:34391; -.
DR   CTD; 390110; -.
DR   GeneCards; ACCSL; -.
DR   HGNC; HGNC:34391; ACCSL.
DR   HPA; ENSG00000205126; Not detected.
DR   neXtProt; NX_Q4AC99; -.
DR   PharmGKB; PA164714805; -.
DR   VEuPathDB; HostDB:ENSG00000205126; -.
DR   eggNOG; KOG0256; Eukaryota.
DR   GeneTree; ENSGT00940000162841; -.
DR   HOGENOM; CLU_017584_1_3_1; -.
DR   InParanoid; Q4AC99; -.
DR   OMA; RRHTQAI; -.
DR   OrthoDB; 1328656at2759; -.
DR   PhylomeDB; Q4AC99; -.
DR   TreeFam; TF354218; -.
DR   PathwayCommons; Q4AC99; -.
DR   SignaLink; Q4AC99; -.
DR   BioGRID-ORCS; 390110; 9 hits in 1135 CRISPR screens.
DR   ChiTaRS; ACCSL; human.
DR   GenomeRNAi; 390110; -.
DR   Pharos; Q4AC99; Tdark.
DR   PRO; PR:Q4AC99; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q4AC99; Protein.
DR   Bgee; ENSG00000205126; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 12 other cell types or tissues.
DR   ExpressionAtlas; Q4AC99; baseline and differential.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR   GO; GO:0006520; P:amino acid metabolic process; IBA:GO_Central.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR43795:SF1; INACTIVE 1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE-LIKE PROTEIN 2-RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   2: Evidence at transcript level;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..568
FT                   /note="Probable inactive 1-aminocyclopropane-1-carboxylate
FT                   synthase-like protein 2"
FT                   /id="PRO_0000337057"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         395
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   VARIANT         529
FT                   /note="C -> R (in dbSNP:rs2074051)"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="VAR_060626"
FT   CONFLICT        192
FT                   /note="S -> R (in Ref. 1; BAE17132)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272
FT                   /note="F -> S (in Ref. 1; BAE17132)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        276
FT                   /note="L -> P (in Ref. 1; BAE17132)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        311
FT                   /note="L -> P (in Ref. 1; BAE17132)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        434
FT                   /note="K -> E (in Ref. 1; BAE17132)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        454
FT                   /note="C -> R (in Ref. 1; BAE17132)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   568 AA;  65249 MW;  233FC638E76AC393 CRC64;
     MSHRSDTLPV PSGQRRGRVP RDHSIYTQLL EITLHLQQAM TEHFVQLTSR QGLSLEERRH
     TEAICEHEAL LSRLICRMIN LLQSGAASGL ELQVPLPSED SRGDVRYGQR AQLSGQPDPV
     PQLSDCEAAF VNRDLSIRGI DISVFYQSSF QDYNAYQKDK YHKDKNTLGF INLGTSENKL
     CMDLMTERLQ ESDMNCIEDT LLQYPDWRGQ PFLREEVARF LTYYCRAPTR LDPENVVVLN
     GCCSVFCALA MVLCDPGEAF LVPAPFYGGF AFSSRLYAKV ELIPVHLESE VTVTNTHPFQ
     LTVDKLEEAL LEARLEGKKV RGLVLINPQN PLGDIYSPDS LMKYLEFAKR YNLHVIIDEI
     YMLSVFDESI TFHSILSMKS LPDSNRTHVI WGTSKDFGIS GFRFGALYTH NKEVASAVSA
     FGYLHSISGI TQHKLCQLLQ NTEWIDKVYL PTNCYRLREA HKYITAELKA LEIPFHNRSS
     GLYVWINLKK YLDPCTFEEE RLLYCRFLDN KLLLSRGKTY MCKEPGWFCL IFADELPRLK
     LAMRRFCDVL QEQKEALIVK QLEDAMRE
//