CMLO1_MOUSE
ID CMLO1_MOUSE Reviewed; 222 AA.
AC Q9JIZ0; Q91XE3; Q9CW77;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable N-acetyltransferase CML1;
DE EC=2.3.1.-;
DE AltName: Full=Camello-like protein 1;
GN Name=Cml1 {ECO:0000312|MGI:MGI:1913366};
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] {ECO:0000312|EMBL:AAF80483.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11397015; DOI=10.1006/dbio.2001.0261;
RA Popsueva A.E., Luchinskaya N.N., Ludwig A.V., Zinovjeva O.Y.,
RA Poteryaev D.A., Feigelman M.M., Ponomarev M.B., Berekelya L.,
RA Belyavsky A.V.;
RT "Overexpression of camello, a member of a novel protein family, reduces
RT blastomere adhesion and inhibits gastrulation in Xenopus laevis.";
RL Dev. Biol. 234:483-496(2001).
RN [2] {ECO:0000312|EMBL:BAB22702.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB22702.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAB22489.1}, and
RC Embryo {ECO:0000312|EMBL:BAB22702.1};
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 [3] {ECO:0000312|EMBL:AAH10796.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH10796.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH10796.1};
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in regulation of gastrulation.
CC {ECO:0000269|PubMed:11397015}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the camello family.
CC {ECO:0000269|PubMed:11397015}.
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DR EMBL; AF163314; AAF80483.1; -; mRNA.
DR EMBL; AK002975; BAB22489.1; -; mRNA.
DR EMBL; AK003301; BAB22702.1; -; mRNA.
DR EMBL; BC010796; AAH10796.1; -; mRNA.
DR CCDS; CCDS20304.3; -.
DR RefSeq; NP_075649.2; NM_023160.2.
DR AlphaFoldDB; Q9JIZ0; -.
DR STRING; 10090.ENSMUSP00000124488; -.
DR iPTMnet; Q9JIZ0; -.
DR PhosphoSitePlus; Q9JIZ0; -.
DR SwissPalm; Q9JIZ0; -.
DR jPOST; Q9JIZ0; -.
DR MaxQB; Q9JIZ0; -.
DR PaxDb; Q9JIZ0; -.
DR PeptideAtlas; Q9JIZ0; -.
DR PRIDE; Q9JIZ0; -.
DR ProteomicsDB; 283445; -.
DR DNASU; 66116; -.
DR Ensembl; ENSMUST00000161198; ENSMUSP00000124488; ENSMUSG00000057103.
DR GeneID; 66116; -.
DR KEGG; mmu:66116; -.
DR CTD; 66116; -.
DR MGI; MGI:1913366; Cml1.
DR VEuPathDB; HostDB:ENSMUSG00000057103; -.
DR eggNOG; KOG3139; Eukaryota.
DR GeneTree; ENSGT00950000182932; -.
DR InParanoid; Q9JIZ0; -.
DR OrthoDB; 1341682at2759; -.
DR PhylomeDB; Q9JIZ0; -.
DR BioGRID-ORCS; 66116; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Nat8f1; mouse.
DR PRO; PR:Q9JIZ0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9JIZ0; protein.
DR Bgee; ENSMUSG00000057103; Expressed in right kidney and 177 other tissues.
DR ExpressionAtlas; Q9JIZ0; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; ISA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISA:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0047198; F:cysteine-S-conjugate N-acetyltransferase activity; ISO:MGI.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; ISO:MGI.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0050435; P:amyloid-beta metabolic process; ISO:MGI.
DR GO; GO:0001702; P:gastrulation with mouth forming second; NAS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISA:MGI.
DR GO; GO:0018003; P:peptidyl-lysine N6-acetylation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Developmental protein; Gastrulation; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..222
FT /note="Probable N-acetyltransferase CML1"
FT /id="PRO_0000284686"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 69..220
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT CONFLICT 196
FT /note="A -> T (in Ref. 3; AAH10796)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 25014 MW; 49EA26BF734782C8 CRC64;
MVPYHIRQYQ DSDHKRVVDV FTKGMEEYIP STFRHMLMLP RTLLLLLGVP LALVLVSGSW
ILAVICIFFL LLLLRLLARQ PWKEYVAKCL QTDMVDITKS YLNVHGACFW VAESGGQVVG
IVAAQPVKDP PLGRKQLQLF RLSVSSQHRG QGIAKALTRT VLQFARDQSY SDVVLETSAL
QQGAVTLYLG MGFKKAGQYF MSIFWRLAGI CTIQLKYSFP SA
