ISM1_DANRE
ID ISM1_DANRE Reviewed; 461 AA.
AC Q5EGE1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Isthmin-1;
DE Flags: Precursor;
GN Name=ism1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=15797017; DOI=10.1016/j.cub.2005.01.041;
RA Weidinger G., Thorpe C.J., Wuennenberg-Stapleton K., Ngai J., Moon R.T.;
RT "The Sp1-related transcription factors sp5 and sp5-like act downstream of
RT Wnt/beta-catenin signaling in mesoderm and neuroectoderm patterning.";
RL Curr. Biol. 15:489-500(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Raible F., Araki I., Brand M.;
RT "Isthmin-1 is regulated by Fgf and TGF beta signalling and contributes to
RT early patterning of the zebrafish embryo.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=19874420; DOI=10.1111/j.1582-4934.2009.00961.x;
RA Xiang W., Ke Z., Zhang Y., Cheng G.H., Irwan I.D., Sulochana K.N.,
RA Potturi P., Wang Z., Yang H., Wang J., Zhuo L., Kini R.M., Ge R.;
RT "Isthmin is a novel secreted angiogenesis inhibitor that inhibits tumour
RT growth in mice.";
RL J. Cell. Mol. Med. 15:359-374(2011).
CC -!- FUNCTION: May specifically influence certain angiogenesis process
CC (PubMed:19874420). {ECO:0000269|PubMed:19874420}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the late gastrulation/early
CC segmentation stage in the midbrain/hindbrain boundary (MHB) and in the
CC posterior trunk region. Subsequently, its expression is restricted in
CC the tail bud region and notochord. At 22 hrs after fertilization (hpf),
CC high level expression is observed in the notochord and MHB. The tail
CC bud expression declined by 30 hpf. Notochord expression declines at 48
CC hpf and disappears by 72 hpf although low level MHB expression remains
CC until 72 hpf (PubMed:19874420). {ECO:0000269|PubMed:19874420}.
CC -!- INDUCTION: Up-regulated by Wnt signaling.
CC {ECO:0000269|PubMed:15797017}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC disorganized intersegmental vessels in the trunk.
CC {ECO:0000269|PubMed:19874420}.
CC -!- SIMILARITY: Belongs to the isthmin family. {ECO:0000305}.
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DR EMBL; AY856371; AAX52519.1; -; mRNA.
DR EMBL; AY884208; AAW79562.1; -; mRNA.
DR EMBL; BC129141; AAI29142.1; -; mRNA.
DR EMBL; BC155303; AAI55304.1; -; mRNA.
DR RefSeq; NP_001012376.1; NM_001012376.1.
DR AlphaFoldDB; Q5EGE1; -.
DR SMR; Q5EGE1; -.
DR STRING; 7955.ENSDARP00000023737; -.
DR PaxDb; Q5EGE1; -.
DR GeneID; 497617; -.
DR KEGG; dre:497617; -.
DR CTD; 140862; -.
DR ZFIN; ZDB-GENE-050523-3; ism1.
DR eggNOG; ENOG502QR6G; Eukaryota.
DR InParanoid; Q5EGE1; -.
DR OrthoDB; 876510at2759; -.
DR PhylomeDB; Q5EGE1; -.
DR PRO; PR:Q5EGE1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0001525; P:angiogenesis; IMP:ZFIN.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:ZFIN.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:ZFIN.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:ZFIN.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IBA:GO_Central.
DR Gene3D; 2.20.100.10; -; 1.
DR InterPro; IPR005533; AMOP_dom.
DR InterPro; IPR042413; ISM.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR10239:SF30; PTHR10239:SF30; 1.
DR Pfam; PF03782; AMOP; 1.
DR Pfam; PF00090; TSP_1; 1.
DR SMART; SM00723; AMOP; 1.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS50856; AMOP; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..461
FT /note="Isthmin-1"
FT /id="PRO_0000348258"
FT DOMAIN 215..259
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 286..449
FT /note="AMOP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00347"
FT REGION 40..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 226..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 230..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 241..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 461 AA; 51176 MW; AC9286A244D6DC80 CRC64;
MVRLAAELLL LLGLLLLTLH ITVLRSSPLQ HGNDTVSLEQ DSRVAENNVN ADSSSSVQLG
PGDRQTRVAH IPASQPWAQS PGTGGSLQRD GPGAFLLDLQ NFPDLSKADI NGQNPNIQVT
IEVVDSLEGS EPEKGMRKEN KPGWAAPNWR NWWQRSSSSS SSSVSTPKGP EEQDYPYESN
TEDSNFLKPL GDWERRVKSE AGAGSRTQTE YDYIDGEGDW SAWSPCSVSC GNGNQKRTRS
CGYACTATES RTCDMPSCPG IEDAFKTAAT EVSLLAGTEE FNATELFGVD TDSCERWMNC
KSEFLKKYMS KVATDLPSCP CFYPTEVAYS TADVHDANTK RNFRWKDASG PKEKLEIYKP
TARYCIRSML TLESTTLAAQ HCCYDDSMKL ITRGKGAGTP NLISTEFSAD LHYKVDILPW
IICKGDWSRY NHARPPNNGQ KCAENPQDED YYKQFEEARE F
