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1A1L1_MOUSE
ID   1A1L1_MOUSE             Reviewed;         502 AA.
AC   A2AIG8; Q8CHS6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase-like protein 1;
DE            Short=ACC synthase-like protein 1;
GN   Name=Accs;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAH39569.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH39569.1};
RC   TISSUE=Mammary gland {ECO:0000312|EMBL:AAH39569.1};
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).
CC   -!- FUNCTION: Does not catalyze the synthesis of 1-aminocyclopropane-1-
CC       carboxylate but is capable of catalyzing the deamination of L-
CC       vinylglycine. {ECO:0000250|UniProtKB:Q96QU6}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2AIG8-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:15489334};
CC         IsoId=A2AIG8-2; Sequence=VSP_052669;
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000255}.
CC   -!- CAUTION: Similar to plant 1-aminocyclopropane-1-carboxylate synthases
CC       but lacks a number of residues which are necessary for activity.
CC       {ECO:0000250|UniProtKB:Q96QU6}.
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DR   EMBL; AL732472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC039569; AAH39569.1; -; mRNA.
DR   CCDS; CCDS16457.1; -. [A2AIG8-2]
DR   CCDS; CCDS71105.1; -. [A2AIG8-1]
DR   RefSeq; NP_001277711.1; NM_001290782.1. [A2AIG8-1]
DR   RefSeq; NP_899043.1; NM_183220.3. [A2AIG8-2]
DR   RefSeq; XP_006499823.1; XM_006499760.2. [A2AIG8-1]
DR   RefSeq; XP_006499824.1; XM_006499761.2. [A2AIG8-1]
DR   RefSeq; XP_006499826.1; XM_006499763.2. [A2AIG8-2]
DR   RefSeq; XP_006499827.1; XM_006499764.2. [A2AIG8-2]
DR   RefSeq; XP_006499828.1; XM_006499765.2. [A2AIG8-2]
DR   RefSeq; XP_006499829.1; XM_006499766.2. [A2AIG8-2]
DR   AlphaFoldDB; A2AIG8; -.
DR   SMR; A2AIG8; -.
DR   STRING; 10090.ENSMUSP00000036268; -.
DR   iPTMnet; A2AIG8; -.
DR   PhosphoSitePlus; A2AIG8; -.
DR   EPD; A2AIG8; -.
DR   MaxQB; A2AIG8; -.
DR   PaxDb; A2AIG8; -.
DR   PeptideAtlas; A2AIG8; -.
DR   PRIDE; A2AIG8; -.
DR   ProteomicsDB; 285528; -. [A2AIG8-1]
DR   ProteomicsDB; 285529; -. [A2AIG8-2]
DR   Antibodypedia; 13193; 206 antibodies from 26 providers.
DR   DNASU; 329470; -.
DR   Ensembl; ENSMUST00000041593; ENSMUSP00000036268; ENSMUSG00000040272. [A2AIG8-2]
DR   Ensembl; ENSMUST00000068513; ENSMUSP00000065389; ENSMUSG00000040272. [A2AIG8-2]
DR   Ensembl; ENSMUST00000111246; ENSMUSP00000106877; ENSMUSG00000040272. [A2AIG8-1]
DR   GeneID; 329470; -.
DR   KEGG; mmu:329470; -.
DR   UCSC; uc008lgj.2; mouse. [A2AIG8-1]
DR   CTD; 84680; -.
DR   MGI; MGI:1919717; Accs.
DR   VEuPathDB; HostDB:ENSMUSG00000040272; -.
DR   eggNOG; KOG0256; Eukaryota.
DR   GeneTree; ENSGT00940000161101; -.
DR   HOGENOM; CLU_017584_1_3_1; -.
DR   InParanoid; A2AIG8; -.
DR   OMA; HGIEYAT; -.
DR   OrthoDB; 1156861at2759; -.
DR   PhylomeDB; A2AIG8; -.
DR   TreeFam; TF354218; -.
DR   BioGRID-ORCS; 329470; 1 hit in 74 CRISPR screens.
DR   PRO; PR:A2AIG8; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; A2AIG8; protein.
DR   Bgee; ENSMUSG00000040272; Expressed in metanephric renal vesicle and 193 other tissues.
DR   ExpressionAtlas; A2AIG8; baseline and differential.
DR   Genevisible; A2AIG8; MM.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..502
FT                   /note="1-aminocyclopropane-1-carboxylate synthase-like
FT                   protein 1"
FT                   /id="PRO_0000318072"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         324
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..23
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_052669"
SQ   SEQUENCE   502 AA;  56879 MW;  9399891308FC91A0 CRC64;
     MFCLPQQEST APTTCTGSAS TQDMDSGYGD GLQGECLRKP DQTQPKLYGV GDPTATFSSD
     SSCLSSRGRV IKWFWDSAEE GYRTYHMDEY DEDKNPSGII NLGTSENKLC FDLLSWRLTQ
     GDMLHVEPSL LQYPDWRGHL FLREEVAKFL SFYCKSPAPL KPENVVVLNG CASLFSALAT
     VLCEAGEALL IPTPYYGAIT QHIYLYGNVR LAYVYLDSKV TGLNTRPFQL TVEKLEMVLQ
     GVSSEGVKVK GLILINPQNP LGDVYSPEEL QDFLRFAMRH KLHVIMDEVY MLSVFEESLG
     YRSVLSLERL PDPQRTHVMW ATSKDFGMSG LRFGVLYTEN QHVATAVASL CRYHGLSGLV
     QHQMAQLLRD HDWISQVYLP ENHARLKAAH TYVSEELRAL GIPFVSRGAG FFIWVDLRKY
     LCKGTFEEEA LLWRQFLDNK VLLSSGKTFE CKEPGWFRVV FSDKENRLRL GMQRMRQVLE
     GQSQVVEDAS PCHAQEPQSQ PR
 
 
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