CMLO_XENLA
ID CMLO_XENLA Reviewed; 219 AA.
AC Q9I8W5;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Probable N-acetyltransferase camello;
DE EC=2.3.1.-;
DE AltName: Full=Xcml;
GN Name=cml {ECO:0000312|EMBL:AAF80482.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF80482.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Gastrula {ECO:0000269|PubMed:11397015};
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: Plays a role in regulation of gastrulation, possibly by
CC controlled reduction of cell adhesion which is necessary for optimal
CC cell motility. {ECO:0000269|PubMed:11397015}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11397015}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11397015}.
CC -!- TISSUE SPECIFICITY: At the beginning of gastrulation, expressed in deep
CC cells of the presumptive mesoderm. At later gastrulation stages,
CC expressed at the interface between already involuted and preinvoluted
CC mesoderm. At late neurula and tailbud stages, expressed in the deep
CC mass of cells lying ventrally and laterally to the closed blastopore.
CC {ECO:0000269|PubMed:11397015}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected after midblastula
CC transition, reaches its maximum at stages 12-15 and continues to be
CC expressed until at least stage 27. {ECO:0000269|PubMed:11397015}.
CC -!- SIMILARITY: Belongs to the camello family.
CC {ECO:0000269|PubMed:11397015}.
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DR EMBL; AF163313; AAF80482.1; -; mRNA.
DR RefSeq; NP_001079090.1; NM_001085621.1.
DR AlphaFoldDB; Q9I8W5; -.
DR SMR; Q9I8W5; -.
DR GeneID; 373623; -.
DR KEGG; xla:373623; -.
DR CTD; 373623; -.
DR Xenbase; XB-GENE-6252886; nat8.6.S.
DR OrthoDB; 1341682at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 373623; Expressed in gastrula and 3 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008080; F:N-acetyltransferase activity; NAS:UniProtKB.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IMP: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; Golgi apparatus;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..219
FT /note="Probable N-acetyltransferase camello"
FT /id="PRO_0000284697"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 62..218
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 219 AA; 25065 MW; 3295779BD9DDAC65 CRC64;
MANVSIRKYK NSDYETVNFL FVEGTKEHLP AACWNTLKKP RFYFIIIVAC ASIFMCTSSY
VLSLTSLVAL LAVGWYGLYL EFHGYASRCQ REDMLDIENS YMMSDNTCFW VAEIDRKVVG
IVGAKPLKEA DDELFLLHLS VARDCRQQRI GTKLCQTVID FARQRGFKAV CLETANIQDA
AIKLYEAVGF KKSLVAIPPF LLNQYTSFTV IYYRYDIKS