ISM2_DANRE
ID ISM2_DANRE Reviewed; 437 AA.
AC Q58T08; Q1JQ38;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Isthmin-2;
DE Flags: Precursor;
GN Name=ism2;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-197.
RC TISSUE=Larva;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the isthmin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI16498.1; Type=Miscellaneous discrepancy; Note=Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AY856372; AAX52520.1; -; mRNA.
DR EMBL; BC116497; AAI16498.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001018345.1; NM_001020509.1.
DR AlphaFoldDB; Q58T08; -.
DR SMR; Q58T08; -.
DR STRING; 7955.ENSDARP00000070453; -.
DR PaxDb; Q58T08; -.
DR PRIDE; Q58T08; -.
DR GeneID; 553163; -.
DR KEGG; dre:553163; -.
DR CTD; 553163; -.
DR ZFIN; ZDB-GENE-050523-4; ism2b.
DR eggNOG; ENOG502RU1R; Eukaryota.
DR InParanoid; Q58T08; -.
DR OrthoDB; 876510at2759; -.
DR PhylomeDB; Q58T08; -.
DR PRO; PR:Q58T08; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:SF28; PTHR10239:SF28; 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..437
FT /note="Isthmin-2"
FT /id="PRO_0000348259"
FT DOMAIN 197..242
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 262..425
FT /note="AMOP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00347"
FT REGION 156..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..176
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 209..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 213..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 224..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 437 AA; 49717 MW; 29EE2B79EC4E0490 CRC64;
MLRARKGLWV LLSVLLAFWI ERAISFPVRH HKRSRNGVYV ENQVQNHLAD SHPHQRRWLQ
HHSTGVLPLP EPEEESKPFV LDFKNLPDLA NADIGSQNPN IQVTIEVLDD PPMDVEMDLV
KEWSNDWSTS SPSSTVEWLG GKKLFWPLFW GYTDADSGED GTGQAEDEED DYDYDSGEPI
PSGLGKTDGD WTHNRYEEKE EEWSTWSPCS VTCGHGNQTR SRSCGDFCTS TESQSCDLVP
CPDDWNSVGH VFPFEMENGT EPYGTDVGSC EKWLNCKSEF LQRYLQQVFT ELPNCPCSYP
SHVSNNIVSL LDVGHERSFQ WRDASGPKER LDIYKPSARS CLRSGLSKNG TTLAAQHCCY
DDNKQLITRG KGAGTPNLIS TEFSPELHFK VDVLPWILCK GDWSRFHAVR PPNNGLHCME
NPQQDIFMNE LEEAREY