1A1L2_MOUSE
ID 1A1L2_MOUSE Reviewed; 580 AA.
AC Q3UX83; Q3TQ30;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Probable inactive 1-aminocyclopropane-1-carboxylate synthase-like protein 2;
DE Short=ACC synthase-like protein 2;
GN Name=Accsl; Synonyms=Gm1967;
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UX83-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UX83-2; Sequence=VSP_033860;
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; AK135828; BAE22680.1; -; mRNA.
DR EMBL; AK163963; BAE37555.1; -; mRNA.
DR EMBL; AL732472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38183.1; -. [Q3UX83-1]
DR RefSeq; NP_001028624.2; NM_001033452.4. [Q3UX83-1]
DR RefSeq; XP_011237948.1; XM_011239646.1.
DR AlphaFoldDB; Q3UX83; -.
DR SMR; Q3UX83; -.
DR STRING; 10090.ENSMUSP00000097281; -.
DR PhosphoSitePlus; Q3UX83; -.
DR PaxDb; Q3UX83; -.
DR PRIDE; Q3UX83; -.
DR ProteomicsDB; 285530; -. [Q3UX83-1]
DR ProteomicsDB; 285531; -. [Q3UX83-2]
DR Antibodypedia; 26088; 48 antibodies from 16 providers.
DR Ensembl; ENSMUST00000099690; ENSMUSP00000097281; ENSMUSG00000075023. [Q3UX83-1]
DR GeneID; 381411; -.
DR KEGG; mmu:381411; -.
DR UCSC; uc008lgl.2; mouse. [Q3UX83-1]
DR CTD; 390110; -.
DR MGI; MGI:3584519; Accsl.
DR VEuPathDB; HostDB:ENSMUSG00000075023; -.
DR eggNOG; KOG0256; Eukaryota.
DR GeneTree; ENSGT00940000162841; -.
DR HOGENOM; CLU_017584_1_3_1; -.
DR InParanoid; Q3UX83; -.
DR OMA; RRHTQAI; -.
DR OrthoDB; 1156861at2759; -.
DR PhylomeDB; Q3UX83; -.
DR TreeFam; TF354218; -.
DR BioGRID-ORCS; 381411; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Accsl; mouse.
DR PRO; PR:Q3UX83; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3UX83; protein.
DR Bgee; ENSMUSG00000075023; Expressed in animal zygote and 27 other tissues.
DR ExpressionAtlas; Q3UX83; baseline and differential.
DR Genevisible; Q3UX83; MM.
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..580
FT /note="Probable inactive 1-aminocyclopropane-1-carboxylate
FT synthase-like protein 2"
FT /id="PRO_0000337058"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 417
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033860"
SQ SEQUENCE 580 AA; 66129 MW; 1C1EF92E805F8FE8 CRC64;
MSENRNEGSS QAAKANSDTQ TPSHFKVTHP RLRDQLKKKS SKKKGFKFVQ EKMLKFQHVI
RNQFLQQISQ QMQCVPPGDQ QCTQTSRKRK KMGYLLSQMV NFLWSNTVKK LKFKVPLPCL
DSRCGIKVGH QTLSPWQTGQ SRPSLGGFEA ALASCTLSKR GAGIYESYHL SFQSYEAYQA
DKYHKDKNPS GYINLSTSEN KLCLDLITAR LTQSDMNLLD EAQLQYSDWK GQPFLREELA
SFLTHYCKAP TPLDPENVVV LNGCSSVFAS LAMVLCDPGD ALLIPTPCYN GFVFSSHLYS
KIELIPVHLE SQVPRSNLDS FQLTVDKLKL ALTQAKKKAK KVKGLVLINP QNPLGDVYTQ
SSLQEYLVFA KTHKLHVIMD EIYMLSVFEP SVTFHSVLSI KDLPDPNMTH MIWGTSKDFG
MSGIRFGVLY THNKEVASAM KAFGYHHGVS GITQYKLCRL LQDKEWISKV YLPKNHSRLQ
KAYSYITKIL KDLKIPFYNG GSGLFVWINL KAYLSPCTFD QEQILHQRFR DKKLLLSSGK
SYMCIEPGWF RLVFAETHLH LQVAMDRFCH VLAEHKKHEK
