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Database: UniProt
Entry: S9WSD1_CAMFR
LinkDB: S9WSD1_CAMFR
Original site: S9WSD1_CAMFR 
ID   S9WSD1_CAMFR            Unreviewed;       177 AA.
AC   S9WSD1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Insulin-like growth factor II {ECO:0000256|ARBA:ARBA00018566};
GN   ORFNames=CB1_001062001 {ECO:0000313|EMBL:EPY78464.1};
OS   Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY78464.1, ECO:0000313|Proteomes:UP000030684};
RN   [1] {ECO:0000313|EMBL:EPY78464.1, ECO:0000313|Proteomes:UP000030684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX   PubMed=23149746;
RG   Bactrian Camels Genome Sequencing and Analysis Consortium;
RA   Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA   Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA   Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA   Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA   Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA   Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA   Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA   Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA   Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA   Bayaer T., Li Y., Meng H.;
RT   "Genome sequences of wild and domestic bactrian camels.";
RL   Nat. Commun. 3:1202-1202(2012).
CC   -!- FUNCTION: Preptin undergoes glucose-mediated co-secretion with insulin,
CC       and acts as a physiological amplifier of glucose-mediated insulin
CC       secretion. Exhibits osteogenic properties by increasing osteoblast
CC       mitogenic activity through phosphoactivation of MAPK1 and MAPK3.
CC       {ECO:0000256|ARBA:ARBA00043916}.
CC   -!- FUNCTION: The insulin-like growth factors possess growth-promoting
CC       activity (By similarity). Major fetal growth hormone in mammals. Plays
CC       a key role in regulating fetoplacental development. IGF2 is influenced
CC       by placental lactogen. Also involved in tissue differentiation. In
CC       adults, involved in glucose metabolism in adipose tissue, skeletal
CC       muscle and liver. Acts as a ligand for integrin which is required for
CC       IGF2 signaling. Positively regulates myogenic transcription factor
CC       MYOD1 function by facilitating the recruitment of transcriptional
CC       coactivators, thereby controlling muscle terminal differentiation (By
CC       similarity). Inhibits myoblast differentiation and modulates metabolism
CC       via increasing the mitochondrial respiration rate.
CC       {ECO:0000256|ARBA:ARBA00025573}.
CC   -!- SUBUNIT: Interacts with MYORG; this interaction is required for IGF2
CC       secretion. Interacts with integrins ITGAV:ITGB3 and ITGA6:ITGB4;
CC       integrin-binding is required for IGF2 signaling.
CC       {ECO:0000256|ARBA:ARBA00011472}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       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; KB017292; EPY78464.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9WSD1; -.
DR   SMR; S9WSD1; -.
DR   Proteomes; UP000030684; Unassembled WGS sequence.
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   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   CDD; cd04368; IlGF; 1.
DR   Gene3D; 1.10.100.10; Insulin-like; 1.
DR   InterPro; IPR022334; IGF2.
DR   InterPro; IPR013576; IGF2_C.
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; PTHR46886; INSULIN-LIKE GROWTH FACTOR II; 1.
DR   PANTHER; PTHR46886:SF1; INSULIN-LIKE GROWTH FACTOR II; 1.
DR   Pfam; PF08365; IGF2_C; 1.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR02002; INSLNLIKEGF.
DR   PRINTS; PR02006; INSLNLIKEGF2.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; Insulin-like; 1.
DR   PROSITE; PS00262; INSULIN; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR622350-50};
KW   Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Growth factor {ECO:0000256|ARBA:ARBA00023030};
KW   Mitogen {ECO:0000256|ARBA:ARBA00023246};
KW   Osteogenesis {ECO:0000256|ARBA:ARBA00022855};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030684};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU000406};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..177
FT                   /note="Insulin-like growth factor II"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004572715"
FT   DOMAIN          26..80
FT                   /note="Insulin-like"
FT                   /evidence="ECO:0000259|SMART:SM00078"
FT   REGION          156..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        29..67
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622350-50"
FT   DISULFID        41..80
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622350-50"
FT   DISULFID        66..71
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622350-50"
SQ   SEQUENCE   177 AA;  19867 MW;  62D8B980F9EE3C57 CRC64;
     MEKSVLVLLA FLAFASCCFA AYRPSETLCG GELVDTLQFV CGDRGFYFSR PASRMSRRSR
     GIVEECCFRS CDLALLETYC ATPAKSERDV STPPTVLPDN FPRYPVGKFF QYDTWKQSAQ
     RLRRGLPALL RARRGRTLAK ELEVFREAKR HRPLIALPNQ DPAAHGGASP EASSNRK
//
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