ISM1_MOUSE
ID ISM1_MOUSE Reviewed; 454 AA.
AC A2ATD1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Isthmin-1;
DE Flags: Precursor;
GN Name=Ism1; Synonyms=Ism;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP IDENTIFICATION.
RX PubMed=12128218; DOI=10.1016/s0925-4773(02)00123-5;
RA Pera E.M., Kim J.I., Martinez S.L., Brechner M., Li S.-Y., Wessely O.,
RA De Robertis E.M.;
RT "Isthmin is a novel secreted protein expressed as part of the Fgf-8
RT synexpression group in the Xenopus midbrain-hindbrain organizer.";
RL Mech. Dev. 116:169-172(2002).
RN [3]
RP FUNCTION, INTERACTION WITH ITGAV/ITGB5, AND DOMAIN.
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: Acts as an angiogenesis inhibitor.
CC {ECO:0000269|PubMed:19874420}.
CC -!- SUBUNIT: Interacts with integrin ITGAV/ITGB5.
CC {ECO:0000269|PubMed:19874420}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DOMAIN: The C-terminal AMOP domain plays an important role in the anti-
CC angiogenic function of ISM1. {ECO:0000269|PubMed:19874420}.
CC -!- SIMILARITY: Belongs to the isthmin family. {ECO:0000305}.
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DR EMBL; AL928831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A2ATD1; -.
DR STRING; 10090.ENSMUSP00000139280; -.
DR iPTMnet; A2ATD1; -.
DR PhosphoSitePlus; A2ATD1; -.
DR PaxDb; A2ATD1; -.
DR PRIDE; A2ATD1; -.
DR ProteomicsDB; 269339; -.
DR Antibodypedia; 52888; 66 antibodies from 13 providers.
DR Ensembl; ENSMUST00000099307; ENSMUSP00000096910; ENSMUSG00000074766.
DR MGI; MGI:2442963; Ism1.
DR VEuPathDB; HostDB:ENSMUSG00000074766; -.
DR eggNOG; ENOG502QR6G; Eukaryota.
DR GeneTree; ENSGT00940000159062; -.
DR HOGENOM; CLU_030263_0_0_1; -.
DR InParanoid; A2ATD1; -.
DR PhylomeDB; A2ATD1; -.
DR TreeFam; TF331333; -.
DR ChiTaRS; Ism1; mouse.
DR PRO; PR:A2ATD1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2ATD1; protein.
DR Bgee; ENSMUSG00000074766; Expressed in stroma of bone marrow and 142 other tissues.
DR ExpressionAtlas; A2ATD1; baseline and differential.
DR Genevisible; A2ATD1; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..454
FT /note="Isthmin-1"
FT /id="PRO_0000348257"
FT DOMAIN 208..252
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 279..442
FT /note="AMOP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00347"
FT REGION 29..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 219..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 223..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 234..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 454 AA; 51145 MW; 5D0724101922CC34 CRC64;
MVRLAAELLL LLGLLLLTLH ITVLRGSGAS DRQDAAAGNN NLNLESDSTS ETSFPLSKEA
PEEHQVVHQP FPRQRFPPET GHPSLQRDGP RSFLLDLPNF PDLSKADING QNPNIQVTIE
VVDGPDSEAE KDQHPENKPS WSLPAPDWRA WWQRSLSLAR TNSGDQDDKY DSTSDDSNFL
SVPRGWDRPA PGHRTFETKE QPEYDSTDGE GDWSLWSVCS VTCGNGNQKR TRSCGYACIA
TESRTCDRPN CPGIEDTFRT AATEVSLLAG SEEFNATKLF EVDMDSCERW MSCKSEFLKK
YMHKVINDLP SCPCSYPTEV AYSTADIFDR IKRKDFRWKD ASGPKEKLEI YKPTARYCIR
SMLSLESTTL AAQHCCYGDN MQLITRGKGA GTPNLISTEF SAELHYKVDV LPWIICKGDW
SRYNEARPPN NGQKCTESPS DEDYIKQFQE AREY
