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