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Database: UniProt
Entry: A9YN29_9TELE
LinkDB: A9YN29_9TELE
Original site: A9YN29_9TELE 
ID   A9YN29_9TELE            Unreviewed;       185 AA.
AC   A9YN29;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Preproinsulin-like growth factor-I {ECO:0000313|EMBL:ABY27564.1};
OS   Odontesthes bonariensis (pejerrey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Atheriniformes; Atherinopsidae;
OC   Atherinopsinae; Odontesthes.
OX   NCBI_TaxID=219752 {ECO:0000313|EMBL:ABY27564.1};
RN   [1] {ECO:0000313|EMBL:ABY27564.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18521839; DOI=10.1002/jez.466;
RA   Sciara A.A., Somoza G.M., Arranz S.E.;
RT   "Insulin-like growth factor-I of pejerrey, Odontesthes bonariensis: cDNA
RT   characterization, tissue distribution and expression profiles after growth
RT   hormone administration.";
RL   J. Exp. Zool. Part A Ecol. Genet. Physiol. 309:407-418(2008).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU000406}.
CC   -!- SIMILARITY: Belongs to the insulin family.
CC       {ECO:0000256|ARBA:ARBA00009034, ECO:0000256|RuleBase:RU000406}.
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DR   EMBL; EU257205; ABY27564.1; -; mRNA.
DR   AlphaFoldDB; A9YN29; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   CDD; cd04368; IlGF; 1.
DR   Gene3D; 1.10.100.10; Insulin-like; 1.
DR   InterPro; IPR022341; IGF-I.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022350; Insulin-like_growth_factor.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   PANTHER; PTHR46845:SF3; INSULIN-LIKE GROWTH FACTOR 1; 1.
DR   PANTHER; PTHR46845; INSULIN-LIKE GROWTH FACTOR I; 1.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR02002; INSLNLIKEGF.
DR   PRINTS; PR02005; INSLNLIKEGF1.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; Insulin-like; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR622350-50};
KW   Growth factor {ECO:0000256|ARBA:ARBA00023030};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU000406};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..43
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           44..185
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002747329"
FT   DOMAIN          47..103
FT                   /note="Insulin-like"
FT                   /evidence="ECO:0000259|SMART:SM00078"
FT   REGION          113..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        50..90
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622350-50"
FT   DISULFID        62..103
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622350-50"
FT   DISULFID        89..94
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622350-50"
SQ   SEQUENCE   185 AA;  20304 MW;  65FD4909933EF92F CRC64;
     MSSAHSSQWH LYDVLKGAMC CISCSHTLSL LLCVLTLTPT ATGAGPETLC GAELVDTLQF
     VCGERGFYFS KPTGYGPNAR RSRGIVDECC FQSCELRRLE MYCAPAKSGK AARSVRSQRH
     TDMPRAPKVS TPGHKVDKGT ERRTAQQPDK TKKKRPLPGH SHSSFKEVHQ KNSSRGSAGG
     KNYRM
//
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