CMLO1_RAT
ID CMLO1_RAT Reviewed; 221 AA.
AC Q9QXT4;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Probable N-acetyltransferase CML1;
DE EC=2.3.1.-;
DE AltName: Full=Camello-like protein 1;
DE AltName: Full=Camello-like protein 2;
GN Name=Cml1 {ECO:0000250|UniProtKB:Q9JIZ0};
GN Synonyms=Cml2 {ECO:0000312|RGD:621606};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAF22297.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAF22297.1};
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).
RN [2] {ECO:0000312|EMBL:AAH78836.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH78836.1};
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).
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; AF185569; AAF22297.1; -; mRNA.
DR EMBL; BC078836; AAH78836.1; -; mRNA.
DR RefSeq; NP_067700.2; NM_021668.3.
DR AlphaFoldDB; Q9QXT4; -.
DR SMR; Q9QXT4; -.
DR STRING; 10116.ENSRNOP00000021167; -.
DR iPTMnet; Q9QXT4; -.
DR PhosphoSitePlus; Q9QXT4; -.
DR PaxDb; Q9QXT4; -.
DR GeneID; 59300; -.
DR KEGG; rno:59300; -.
DR UCSC; RGD:621606; rat.
DR CTD; 66116; -.
DR RGD; 621606; Cml1.
DR eggNOG; KOG3139; Eukaryota.
DR InParanoid; Q9QXT4; -.
DR OrthoDB; 1341682at2759; -.
DR PhylomeDB; Q9QXT4; -.
DR TreeFam; TF324687; -.
DR PRO; PR:Q9QXT4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0001702; P:gastrulation with mouth forming second; NAS:UniProtKB.
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..221
FT /note="Probable N-acetyltransferase CML1"
FT /id="PRO_0000284687"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 69..219
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 221 AA; 24857 MW; 754357E00DFC079F CRC64;
MAPYHIRQYQ DSDHKSVVDV FTKGMEEHIP STFRHMLMLP RTLLLLLGVP LALVLVSGSW
LLAVVCIFFL LLLLRFLAGQ PWKEYVATCL RTDMADITKS YLNAHGSFWV AESGNQVVGI
VAALPVKDPP SGRKQLQLFR LSVSSQHRGQ GIAKALVRTV LQFARDQGYT DVVLETSTLQ
QGAMTLYLGM GFQKTGQRFL TMFWRLVGIR TIQLKYPFPS A