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ESM1_RAT
ID   ESM1_RAT                Reviewed;         184 AA.
AC   P97682;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Endothelial cell-specific molecule 1;
DE            Short=ESM-1;
DE   AltName: Full=PG25;
DE   Flags: Precursor;
GN   Name=Esm1;
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].
RC   STRAIN=Sprague-Dawley; TISSUE=Pineal gland;
RX   PubMed=9196290; DOI=10.1016/s0165-0270(97)02237-1;
RA   Wang X., Brownstein M.J., Young W.S.;
RT   "PG25, a pineal-specific cDNA, cloned by differential display PCR (DDPCR)
RT   and rapid amplification of cDNA ends (RACE).";
RL   J. Neurosci. Methods 73:187-191(1997).
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: Involved in angiogenesis; promotes angiogenic sprouting. May
CC       have potent implications in lung endothelial cell-leukocyte
CC       interactions (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Pineal gland specific.
CC   -!- PTM: O-glycosylated; contains chondroitin sulfate and dermatan sulfate.
CC       {ECO:0000250}.
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DR   EMBL; U80818; AAB39192.1; -; mRNA.
DR   EMBL; BC070888; AAH70888.1; -; mRNA.
DR   RefSeq; NP_072126.1; NM_022604.2.
DR   AlphaFoldDB; P97682; -.
DR   STRING; 10116.ENSRNOP00000014559; -.
DR   GlyGen; P97682; 1 site.
DR   PaxDb; P97682; -.
DR   Ensembl; ENSRNOT00000014559; ENSRNOP00000014559; ENSRNOG00000010797.
DR   GeneID; 64536; -.
DR   KEGG; rno:64536; -.
DR   CTD; 11082; -.
DR   RGD; 71013; Esm1.
DR   eggNOG; KOG1218; Eukaryota.
DR   GeneTree; ENSGT00390000018810; -.
DR   HOGENOM; CLU_103395_0_0_1; -.
DR   InParanoid; P97682; -.
DR   OMA; GMECKQT; -.
DR   OrthoDB; 1508747at2759; -.
DR   PhylomeDB; P97682; -.
DR   PRO; PR:P97682; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000010797; Expressed in adult mammalian kidney and 16 other tissues.
DR   Genevisible; P97682; RN.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005171; F:hepatocyte growth factor receptor binding; ISO:RGD.
DR   GO; GO:0005178; F:integrin binding; ISO:RGD.
DR   GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:1902204; P:positive regulation of hepatocyte growth factor receptor signaling pathway; ISO:RGD.
DR   GO; GO:0002040; P:sprouting angiogenesis; ISO:RGD.
DR   InterPro; IPR038850; ESM1.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000867; IGFBP-like.
DR   PANTHER; PTHR15428; PTHR15428; 1.
DR   Pfam; PF00219; IGFBP; 1.
DR   SMART; SM00121; IB; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS51323; IGFBP_N_2; 1.
PE   2: Evidence at transcript level;
KW   Angiogenesis; Glycoprotein; Proteoglycan; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..184
FT                   /note="Endothelial cell-specific molecule 1"
FT                   /id="PRO_0000014396"
FT   DOMAIN          24..102
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   REGION          145..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        157
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   184 AA;  20075 MW;  58549D713E88E189 CRC64;
     MKSLLLLTTL LIPLHLGMAW SAKYAVDCPE HCDNTECRSS LRCKRTVLDD CGCCQVCAAG
     PGETCYRTVS GMDGVKCGPG LKCHFYSEED DFGDEFGVCK DCPYGTFGMD CKETCNCQSG
     ICDRVTGRCL DFPFFQYAAA KSPSRTSASQ TERDAASGDG NAVREEIGDR NAARPSVMKW
     LNPR
 
 
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