ASND1_MOUSE
ID ASND1_MOUSE Reviewed; 627 AA.
AC Q8BFS9; Q3THX2; Q3U2Y8; Q3U317; Q8BM66; Q91YY3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Asparagine synthetase domain-containing protein 1;
GN Name=Asnsd1;
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=BALB/cJ, C57BL/6J, and NOD; TISSUE=Embryo, and Testis;
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 MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BFS9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BFS9-2; Sequence=VSP_032353;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28818.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE33002.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK031295; BAC27337.1; -; mRNA.
DR EMBL; AK034746; BAC28818.1; ALT_FRAME; mRNA.
DR EMBL; AK049194; BAC33602.1; -; mRNA.
DR EMBL; AK076793; BAC36483.1; -; mRNA.
DR EMBL; AK154984; BAE32973.1; -; mRNA.
DR EMBL; AK155030; BAE33002.1; ALT_FRAME; mRNA.
DR EMBL; AK168103; BAE40074.1; -; mRNA.
DR EMBL; AK170510; BAE41847.1; -; mRNA.
DR EMBL; BC013617; AAH13617.1; -; mRNA.
DR CCDS; CCDS14954.1; -. [Q8BFS9-1]
DR RefSeq; NP_598489.2; NM_133728.3. [Q8BFS9-1]
DR AlphaFoldDB; Q8BFS9; -.
DR SMR; Q8BFS9; -.
DR STRING; 10090.ENSMUSP00000027264; -.
DR iPTMnet; Q8BFS9; -.
DR PhosphoSitePlus; Q8BFS9; -.
DR EPD; Q8BFS9; -.
DR PaxDb; Q8BFS9; -.
DR PeptideAtlas; Q8BFS9; -.
DR PRIDE; Q8BFS9; -.
DR ProteomicsDB; 265118; -. [Q8BFS9-1]
DR ProteomicsDB; 265119; -. [Q8BFS9-2]
DR DNASU; 70396; -.
DR Ensembl; ENSMUST00000027264; ENSMUSP00000027264; ENSMUSG00000026095. [Q8BFS9-1]
DR Ensembl; ENSMUST00000144660; ENSMUSP00000139404; ENSMUSG00000099913. [Q8BFS9-2]
DR GeneID; 70396; -.
DR KEGG; mmu:70396; -.
DR UCSC; uc007azg.2; mouse. [Q8BFS9-1]
DR CTD; 54529; -.
DR MGI; MGI:1917646; Asnsd1.
DR VEuPathDB; HostDB:ENSMUSG00000026095; -.
DR VEuPathDB; HostDB:ENSMUSG00000099913; -.
DR eggNOG; KOG0573; Eukaryota.
DR GeneTree; ENSGT00390000012446; -.
DR HOGENOM; CLU_012368_2_0_1; -.
DR InParanoid; Q8BFS9; -.
DR OMA; LEMDWQR; -.
DR PhylomeDB; Q8BFS9; -.
DR TreeFam; TF314578; -.
DR BioGRID-ORCS; 70396; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q8BFS9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BFS9; protein.
DR Bgee; ENSMUSG00000026095; Expressed in spermatocyte and 72 other tissues.
DR ExpressionAtlas; Q8BFS9; baseline and differential.
DR Genevisible; Q8BFS9; MM.
DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0006529; P:asparagine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01991; Asn_Synthase_B_C; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR001962; Asn_synthase.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00733; Asn_synthase; 1.
DR Pfam; PF13537; GATase_7; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Amino-acid biosynthesis; Asparagine biosynthesis;
KW Glutamine amidotransferase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..627
FT /note="Asparagine synthetase domain-containing protein 1"
FT /id="PRO_0000324762"
FT DOMAIN 2..184
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 308..597
FT /note="Asparagine synthetase"
FT REGION 373..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT VAR_SEQ 547..627
FT /note="PFLDENVVSFLNSLPVWEKVDLTLPRGVGEKLILRLAAMELGLPASALLPKR
FT AIQFGSRIAKLEKSNEKASDKCGRLQILP -> AQHVPVPFATSLTMHMLSDFC (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032353"
FT CONFLICT 39
FT /note="L -> I (in Ref. 1; BAE40074)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="G -> D (in Ref. 1; BAE40074)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="P -> Q (in Ref. 1; BAE40074)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="S -> F (in Ref. 2; AAH13617)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 627 AA; 69753 MW; F21D737EC1B81F6D CRC64;
MCGICCSVSF SIEHFSKELK EDLLHNLRRR GPNSSRQLLK SAVNYQCLFS GHVLHLRGVL
TIQPVEDEHG NVFLWNGEVF NGVKVEAEDN DTQVMFNSLS ACKNESEILL LFSKVQGPWS
FIYYQASSHH LWFGRDFFGR RSLLWQFSNL GKSFCLSSVG TQVYGVADQW QEVPASGIFQ
IDLNSAAVSR SVILKLYPWR YISKEDIAEE CGNDLTQTPA GLPEFVSVVI NEANLYLSKP
VVPLNKKLPE SPLEIQCRNS SSTSGTRETL EVFLTDEHTK KIVQQFIAIL NVSVKRRILC
LAREENLASK EVLKTCSSKA NIAILFSGGV DSMVIAALAD RHIPLDEPID LLNVAFVPKQ
KTGLPIPNIE RKQQNHHEIP SEESSQSPAA DEGPGEAEVP DRVTGKAGLK ELQSVNPSRT
WNFVEINVSL EELQKLRRAR ICHLVQPLDT VLDDSIGCAV WFASRGIGWL VTQDAVRSYK
SSAKVILTGI GADEQLAGYS RHRARFQSLG LEGLNEEIAM ELGRISSRNL GRDDRVIGDH
GKEARFPFLD ENVVSFLNSL PVWEKVDLTL PRGVGEKLIL RLAAMELGLP ASALLPKRAI
QFGSRIAKLE KSNEKASDKC GRLQILP
