位置:首页 > 蛋白库 > CMLO_XENLA
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024