SATL1_MOUSE
ID SATL1_MOUSE Reviewed; 744 AA.
AC Q9D5N8; B9EHI8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Spermidine/spermine N(1)-acetyltransferase-like protein 1;
DE EC=2.3.1.-;
GN Name=Satl1;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 313-744.
RC STRAIN=C57BL/6J; TISSUE=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).
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29707.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL672033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC138011; AAI38012.1; -; mRNA.
DR EMBL; AK015086; BAB29707.1; ALT_INIT; mRNA.
DR CCDS; CCDS53173.1; -.
DR RefSeq; NP_082931.1; NM_028655.1.
DR AlphaFoldDB; Q9D5N8; -.
DR SMR; Q9D5N8; -.
DR STRING; 10090.ENSMUSP00000026601; -.
DR iPTMnet; Q9D5N8; -.
DR PhosphoSitePlus; Q9D5N8; -.
DR PaxDb; Q9D5N8; -.
DR PRIDE; Q9D5N8; -.
DR ProteomicsDB; 256732; -.
DR Antibodypedia; 54033; 61 antibodies from 14 providers.
DR Ensembl; ENSMUST00000026601; ENSMUSP00000026601; ENSMUSG00000025527.
DR GeneID; 73809; -.
DR KEGG; mmu:73809; -.
DR UCSC; uc009udi.2; mouse.
DR CTD; 340562; -.
DR MGI; MGI:1921059; Satl1.
DR VEuPathDB; HostDB:ENSMUSG00000025527; -.
DR eggNOG; KOG3216; Eukaryota.
DR GeneTree; ENSGT00950000183121; -.
DR HOGENOM; CLU_432730_0_0_1; -.
DR InParanoid; Q9D5N8; -.
DR OMA; WDPEYSG; -.
DR OrthoDB; 1228251at2759; -.
DR PhylomeDB; Q9D5N8; -.
DR TreeFam; TF319736; -.
DR BioGRID-ORCS; 73809; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q9D5N8; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9D5N8; protein.
DR Bgee; ENSMUSG00000025527; Expressed in morula and 9 other tissues.
DR ExpressionAtlas; Q9D5N8; baseline and differential.
DR Genevisible; Q9D5N8; MM.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039533; Satl1.
DR PANTHER; PTHR10545:SF60; PTHR10545:SF60; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..744
FT /note="Spermidine/spermine N(1)-acetyltransferase-like
FT protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000282929"
FT DOMAIN 578..735
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 601..602
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 665
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 667..669
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 675..680
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 699..701
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 725
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 317..319
FT /note="YSM -> SSL (in Ref. 3; BAB29707)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="Q -> H (in Ref. 3; BAB29707)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="K -> Q (in Ref. 3; BAB29707)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="D -> N (in Ref. 3; BAB29707)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 744 AA; 83276 MW; E3529D8C7965A5D0 CRC64;
MDQPGTYQSG MTQPSVSQPA MSPPGLSPHN MQQPGTSQPY MNQPSMNQPA MNEPGVTIPD
SSQSDINQAG QSQPNMKQPW SSTNQPGIYK TDMSQLGMKQ PSASQAGMSQ AGMWQPGPPT
SDMKTINPWQ WDPEYSGREP SDTWQITQSN QGTGQSDTVQ EDPSCAEQKQ PDTWKQDPSF
PGMKKTEPWQ WESSPPSVRQ IDAWKWDPDH PGSNQLNLWQ PQLSDSSTRQ FDLRQAGPIE
LGKKESDTWQ LVPSQQGKTP SSSGQQDPSQ QIVRHAVTWQ TGPSPLAKTL SGPWHIGLNQ
SGMEQLNTCQ TGFGQRYSMC QSSGSQSSMK EFHMLQSGSN QPDMNDVDVW QSGTSQPGMH
QMDPWQWGHN YSGNTQSGQW TPGPNALVVG QFDSWQPVQP GMKYSESGPW SPRHLDMRQP
SPSQLATRQF DKWQQNPSMP GVRQLYTWQP TSSFSDTRQL EKFHPCPINL NMEQFWEAVS
RQPGTTQLGT NQLDTNQPDG TQSSQGGKTQ SDKLEPSPRK PEMKGSQPDT SQSDSDHLDI
SQPGPSQLEP GESSMSDLNE SQQRITQSPM GKKDSCSFFI RPAEPEDCPD ILRLIKELAS
YEGMEEKVSL TERDLFRDGF GDNPLFYCLV AEAPSEQTES GVKTIGFAMY YFTYDPRIGK
LLHLEDFYIT EDYQGIGIGA DMLKKLSQIA INTECCGMQF LVIIWNQDSV EYYTRLGALD
LSCEEGWHLF RFNLDDLLEL AEEE
