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Database: UniProt
Entry: A2IT63_ANAPL
LinkDB: A2IT63_ANAPL
Original site: A2IT63_ANAPL 
ID   A2IT63_ANAPL            Unreviewed;       153 AA.
AC   A2IT63;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=Insulin like growth factor 1 {ECO:0000313|Ensembl:ENSAPLP00020026579.1};
DE   SubName: Full=Insulin-like growth factor-I {ECO:0000313|EMBL:BAB69036.1};
GN   Name=IGF-I {ECO:0000313|EMBL:BAB69036.1};
GN   Synonyms=IGF1 {ECO:0000313|Ensembl:ENSAPLP00020026579.1};
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839 {ECO:0000313|EMBL:BAB69036.1};
RN   [1] {ECO:0000313|EMBL:BAB69036.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Cherry valley {ECO:0000313|EMBL:BAB69036.1};
RA   Kansaku N., Yagi E., Nakada A., Okabayashi H., Guemene D., Zadworny D.;
RT   "Molecular cloning of insulin-like growth factor-I complimentary DNA and
RT   promoter region in the domestic duck (Anas platyrhynchos).";
RL   Anim. Sci. J. 74:277-282(2003).
RN   [2] {ECO:0000313|Ensembl:ENSAPLP00020026579.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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; AB061721; BAB69036.1; -; mRNA.
DR   RefSeq; XP_005022610.1; XM_005022553.2.
DR   SMR; A2IT63; -.
DR   Ensembl; ENSAPLT00020028626.1; ENSAPLP00020026579.1; ENSAPLG00020018102.1.
DR   GeneID; 101793597; -.
DR   KEGG; apla:101793597; -.
DR   CTD; 3479; -.
DR   HOGENOM; CLU_123939_0_0_1; -.
DR   OMA; NECCFQS; -.
DR   OrthoDB; 5402912at2759; -.
DR   Proteomes; UP000694400; Chromosome 1.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; ISS:AgBase.
DR   GO; GO:0090277; P:positive regulation of peptide hormone secretion; ISS:AgBase.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:AgBase.
DR   GO; GO:1990418; P:response to insulin-like growth factor stimulus; ISS:AgBase.
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; INSULIN-LIKE GROWTH FACTOR I; 1.
DR   PANTHER; PTHR46845:SF1; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU000406};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          51..109
FT                   /note="Insulin-like"
FT                   /evidence="ECO:0000259|SMART:SM00078"
FT   REGION          119..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        54..96
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622350-50"
FT   DISULFID        66..109
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622350-50"
FT   DISULFID        95..100
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622350-50"
SQ   SEQUENCE   153 AA;  17295 MW;  9195AD9D60164072 CRC64;
     MEKINSLSTQ LVKCCFCDFL KVKMHTVSYI HFFYLGLCLL TLTSSVAAGP ETLCGAELVD
     ALQFVCGDRG FYFSKPTGYG SSSRRLHHKG IVDECCFQSC DLRRLEMYCA PIKPPKSARS
     VRAQRHTDMP KAQKEVHLKN TSRGNTGNRN YRM
//
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