ID   ISM_XENLA               Reviewed;         449 AA.
AC   Q8QFV1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Isthmin;
DE   Flags: Precursor;
GN   Name=ism1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as an angiogenesis inhibitor.
CC       {ECO:0000250|UniProtKB:A2ATD1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at the 4-cell stage embryo. Expressed at
CC       gastrula stage in the ventral blastopore lip and the anterior end of
CC       the notochord. Expressed at early neurula stage throughout the
CC       notochord, the posterior paraxial mesoderm, cranial neural crest,
CC       anterior edge of the neural plate and at the prospective midbrain-
CC       hindbrain boundary (MHB) or isthmus organizer. Expressed at late
CC       neurula stage in the posterior neural fold. Expressed at early tailbud
CC       stage at the MHB until tadpole stage. Expressed at tailbud stage in the
CC       branchial arches, ear placode and ventral mesoderm.
CC       {ECO:0000269|PubMed:12128218}.
CC   -!- DOMAIN: The C-terminal AMOP domain plays an important role in the anti-
CC       angiogenic function of ISM1. {ECO:0000250|UniProtKB:A2ATD1}.
CC   -!- SIMILARITY: Belongs to the isthmin family. {ECO:0000305}.
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DR   EMBL; AY091635; AAM13976.1; -; mRNA.
DR   EMBL; BC160753; AAI60753.1; -; mRNA.
DR   RefSeq; NP_001082228.1; NM_001088759.1.
DR   AlphaFoldDB; Q8QFV1; -.
DR   SMR; Q8QFV1; -.
DR   PRIDE; Q8QFV1; -.
DR   GeneID; 398306; -.
DR   KEGG; xla:398306; -.
DR   CTD; 398306; -.
DR   Xenbase; XB-GENE-963588; ism1.L.
DR   OMA; CYDDSMQ; -.
DR   OrthoDB; 876510at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 398306; Expressed in blastula and 16 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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..449
FT                   /note="Isthmin"
FT                   /id="PRO_0000348260"
FT   DOMAIN          203..247
FT                   /note="TSP type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          274..437
FT                   /note="AMOP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00347"
FT   REGION          27..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        214..241
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        218..246
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        229..233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ   SEQUENCE   449 AA;  50975 MW;  C0606CC927568AB8 CRC64;
     MLRLAAELLL LLGLLLLTLH ITVLRGSPDS SSNSSHSLIQ NEPSSDSFSF NPSDRQEYLD
     EATRRAFPKH RLMTSGHTSL QRDGTGSFLL DLPNFPDLSK VDINGQNPNI QVTIEVVDGP
     DSEPENEMQK ENMPSWPVPS PDWRSWWQRS ATLPRMNYGD QDYKYDSTTE DSNFLNPLGG
     RNRQVPSHRT FDTKEQPEYD YVDGEGDWSS WSVCSVTCGS GNQKRTRTCG YACTATESRT
     CDMPNCPGIE DTFRTAATEV SLLAGNEDFN ATKLFGVDTD SCERWMNCKS EFLKKYMHKV
     ANDLPSCPCS YPTEVAYSTA EIYDRIKRKD FRWKDASGPK EKLEIYKPTA RYCIRSMLSL
     ESTTLAAQHC CFDDSMQLIT RGKGAGTPNL ISVEFSAELH YKVDILPWIM CKGDWSRYNE
     VRPPNNGQKC TENPSEDDYL KQFQEAREF