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MSLN_RAT
ID   MSLN_RAT                Reviewed;         625 AA.
AC   Q9ERA7; Q6IRG1;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Mesothelin;
DE   AltName: Full=Pre-pro-megakaryocyte-potentiating factor;
DE   AltName: Full=Protein expressed in renal carcinoma;
DE   Contains:
DE     RecName: Full=Megakaryocyte-potentiating factor;
DE              Short=MPF;
DE   Contains:
DE     RecName: Full=Mesothelin, cleaved form;
DE   Flags: Precursor;
GN   Name=Msln; Synonyms=Erc, Mpf;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=10944454; DOI=10.1006/bbrc.2000.3280;
RA   Yamashita Y., Yokoyama M., Kobayashi E., Takai S., Hino O.;
RT   "Mapping and determination of the cDNA sequence of the Erc gene
RT   preferentially expressed in renal cell carcinoma in the Tsc2 gene mutant
RT   (Eker) rat model.";
RL   Biochem. Biophys. Res. Commun. 275:134-140(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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: Membrane-anchored forms may play a role in cellular adhesion.
CC       {ECO:0000250}.
CC   -!- FUNCTION: Megakaryocyte-potentiating factor (MPF) may potentiate
CC       megakaryocyte colony formation. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with MUC16. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}. Golgi apparatus {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Megakaryocyte-potentiating factor]: Secreted
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in lung. Overexpressed in
CC       hereditary renal carcinoma developed by Eker rats.
CC       {ECO:0000269|PubMed:10944454}.
CC   -!- PTM: Proteolytically cleaved by a furin-like convertase to generate
CC       megakaryocyte-potentiating factor (MPF), and the cleaved form of
CC       mesothelin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the mesothelin family. {ECO:0000305}.
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DR   EMBL; D87351; BAB13512.1; -; mRNA.
DR   EMBL; BC070934; AAH70934.1; -; mRNA.
DR   PIR; JC7362; JC7362.
DR   RefSeq; NP_113846.1; NM_031658.1.
DR   RefSeq; XP_006246083.1; XM_006246021.3.
DR   RefSeq; XP_006246084.1; XM_006246022.2.
DR   AlphaFoldDB; Q9ERA7; -.
DR   SMR; Q9ERA7; -.
DR   STRING; 10116.ENSRNOP00000026395; -.
DR   GlyGen; Q9ERA7; 3 sites.
DR   PaxDb; Q9ERA7; -.
DR   GeneID; 60333; -.
DR   KEGG; rno:60333; -.
DR   UCSC; RGD:69333; rat.
DR   CTD; 10232; -.
DR   RGD; 69333; Msln.
DR   VEuPathDB; HostDB:ENSRNOG00000019445; -.
DR   eggNOG; ENOG502QRX1; Eukaryota.
DR   HOGENOM; CLU_014552_3_0_1; -.
DR   InParanoid; Q9ERA7; -.
DR   OMA; DFTCTEV; -.
DR   OrthoDB; 459771at2759; -.
DR   PhylomeDB; Q9ERA7; -.
DR   TreeFam; TF331713; -.
DR   Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR   PRO; PR:Q9ERA7; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000019445; Expressed in pancreas and 17 other tissues.
DR   Genevisible; Q9ERA7; RN.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0031016; P:pancreas development; IEP:RGD.
DR   InterPro; IPR010335; Mesothelin.
DR   InterPro; IPR026664; Stereocilin-rel.
DR   PANTHER; PTHR23412; PTHR23412; 1.
DR   Pfam; PF06060; Mesothelin; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW   Disulfide bond; Glycoprotein; Golgi apparatus; GPI-anchor; Lipoprotein;
KW   Membrane; Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..600
FT                   /note="Mesothelin"
FT                   /id="PRO_0000253566"
FT   CHAIN           36..288
FT                   /note="Megakaryocyte-potentiating factor"
FT                   /id="PRO_0000253567"
FT   CHAIN           298..600
FT                   /note="Mesothelin, cleaved form"
FT                   /id="PRO_0000253568"
FT   PROPEP          601..625
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000253569"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13421"
FT   LIPID           600
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        488
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        304..328
FT                   /evidence="ECO:0000250"
FT   CONFLICT        70
FT                   /note="M -> T (in Ref. 1; BAB13512)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   625 AA;  68883 MW;  3ECEF77F88BE2127 CRC64;
     MALPTAQPLL GSCGSPICSR SFLLLLLSLG WLPLLQTQTT RTSQEAALLH AVTGTVDFAS
     LPTGLFLGLM CDEVSGLSMG HAKELAMAVR QKNIVLQVHQ LRCLARRLPK HLTNEELDAL
     PLDLLLFLNP AMFPGQQACA HFFSLISKAN VNVLPRRSLE RQRLLTGALK CQGVYGFQVS
     ETDARALGGL ACDLPGEFVA KSSEVLLPWL ARCGGPLDQG QAKAVREVLR SGRAPYGPPS
     TWSVSTLDAL QGLLVVLDES IVHSIPKDVI TEWLQGISRE PSRLGSKWTV THPRFRRDTE
     QKACPPGKEP NVVDENLIFY QNWELEACVD GTLLAGQMDL VNEIPFTYEQ LSIFKHKLDK
     TYPQGYPESL IKQLGHFFRY VSPEDIRQWN VTSPDTVNTL LKVSKGQKMD AQVIALVACY
     LRGGGKLDED IVKALDNIPL SYLCDFSPQD LHAIPSSVMW LVGLHDLDKC SQRHLGILYQ
     KACSAFQNVS GLEYFEKIRT FLGGASREDL RALSQHNVSM DIATFKKLQV DALVGLSVAE
     VQKLLGPHIG DLKTEEDKSP VRDWLFRQQQ KDLDSLGLGL QGGIPNGYLI LDFNVREAFS
     SGAPLLGPGF VFAWIPALLS ALRLS
 
 
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