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CMLO5_MOUSE
ID   CMLO5_MOUSE             Reviewed;         227 AA.
AC   Q9QXS8; Q8R1G0; Q9D8Z0;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Probable N-acetyltransferase CML5;
DE            EC=2.3.1.-;
DE   AltName: Full=Camello-like protein 5;
GN   Name=Cml5 {ECO:0000312|EMBL:AAH24605.1};
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:BAB25091.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB25091.1};
RC   TISSUE=Pancreas {ECO:0000312|EMBL:BAB25091.1};
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   [2] {ECO:0000312|EMBL:AAH24605.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N {ECO:0000312|EMBL:AAH24605.1};
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH24605.1};
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   [3] {ECO:0000305, ECO:0000312|EMBL:AAF22301.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 97-227.
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAF22301.1};
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).
CC   -!- FUNCTION: May play a role in regulation of gastrulation.
CC       {ECO:0000269|PubMed:11397015}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the camello family.
CC       {ECO:0000269|PubMed:11397015}.
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DR   EMBL; AK007530; BAB25091.1; -; mRNA.
DR   EMBL; BC024605; AAH24605.1; -; mRNA.
DR   EMBL; AF187099; AAF22301.1; -; mRNA.
DR   CCDS; CCDS20300.1; -.
DR   RefSeq; NP_075982.2; NM_023493.2.
DR   AlphaFoldDB; Q9QXS8; -.
DR   STRING; 10090.ENSMUSP00000032074; -.
DR   iPTMnet; Q9QXS8; -.
DR   PhosphoSitePlus; Q9QXS8; -.
DR   jPOST; Q9QXS8; -.
DR   MaxQB; Q9QXS8; -.
DR   PaxDb; Q9QXS8; -.
DR   PeptideAtlas; Q9QXS8; -.
DR   PRIDE; Q9QXS8; -.
DR   ProteomicsDB; 283638; -.
DR   DNASU; 69049; -.
DR   Ensembl; ENSMUST00000032074; ENSMUSP00000032074; ENSMUSG00000079494.
DR   GeneID; 69049; -.
DR   KEGG; mmu:69049; -.
DR   UCSC; uc009cqg.2; mouse.
DR   CTD; 69049; -.
DR   MGI; MGI:1916299; Cml5.
DR   VEuPathDB; HostDB:ENSMUSG00000079494; -.
DR   eggNOG; KOG3139; Eukaryota.
DR   GeneTree; ENSGT00950000182932; -.
DR   HOGENOM; CLU_013985_10_1_1; -.
DR   InParanoid; Q9QXS8; -.
DR   OMA; IQLSAMG; -.
DR   OrthoDB; 1341682at2759; -.
DR   PhylomeDB; Q9QXS8; -.
DR   TreeFam; TF324687; -.
DR   BioGRID-ORCS; 69049; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Nat8f5; mouse.
DR   PRO; PR:Q9QXS8; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9QXS8; protein.
DR   Bgee; ENSMUSG00000079494; Expressed in right kidney and 37 other tissues.
DR   Genevisible; Q9QXS8; MM.
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: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:0007368; P:determination of left/right symmetry; IMP: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:0007507; P:heart development; IMP: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   2: Evidence at transcript level;
KW   Acyltransferase; Developmental protein; Gastrulation; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..227
FT                   /note="Probable N-acetyltransferase CML5"
FT                   /id="PRO_0000284694"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          69..213
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   CONFLICT        99
FT                   /note="R -> K (in Ref. 2; AAH24605 and 3; AAF22301)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        211
FT                   /note="S -> F (in Ref. 3; AAF22301)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221..222
FT                   /note="ST -> FI (in Ref. 3; AAF22301)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   227 AA;  25735 MW;  3E7DCC89F30A6A3C CRC64;
     MAPYQIRQYQ ERDYKLVVGL FSRGMMEHIP AAFRYTLLLP QTLLFLFVMP LTIVLVFGSW
     LLAVICIFFL LLLLRLLAGQ PFKDYVAQCL QTDMADITRS YLNAHGSFWV AESGGLVVGT
     VGGLPVKDPP LGRKQMQLFH LSVSSQHRGQ GIAKALVRTV FQFARDQGYS DVVLETSVIQ
     QSAITLYEAM GFQRTGKYSE ISIIKWLITF SIIHFTYSFP STQKHEL
 
 
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