ID   A0A2K6A0R3_MANLE        Unreviewed;       122 AA.
AC   A0A2K6A0R3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Somatotropin {ECO:0008006|Google:ProtNLM};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000033655.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000033655.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Plays an important role in growth control. Its major role in
CC       stimulating body growth is to stimulate the liver and other tissues to
CC       secrete IGF-1. It stimulates both the differentiation and proliferation
CC       of myoblasts. It also stimulates amino acid uptake and protein
CC       synthesis in muscle and other tissues. {ECO:0000256|ARBA:ARBA00025313}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|RuleBase:RU003618}.
CC   -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC       {ECO:0000256|ARBA:ARBA00008474, ECO:0000256|RuleBase:RU003618}.
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DR   AlphaFoldDB; A0A2K6A0R3; -.
DR   Ensembl; ENSMLET00000057239.1; ENSMLEP00000033655.1; ENSMLEG00000041013.1.
DR   GeneTree; ENSGT00950000182818; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.10; -; 2.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR001400; Somatotropin/Prolactin.
DR   InterPro; IPR018116; Somatotropin_CS.
DR   PANTHER; PTHR11417:SF2; SOMATOTROPIN; 1.
DR   PANTHER; PTHR11417; SOMATOTROPIN,PROLACTIN; 1.
DR   Pfam; PF00103; Hormone_1; 1.
DR   PRINTS; PR00836; SOMATOTROPIN.
DR   SUPFAM; SSF47266; 4-helical cytokines; 2.
DR   PROSITE; PS00338; SOMATOTROPIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hormone {ECO:0000256|ARBA:ARBA00022702, ECO:0000256|RuleBase:RU003618};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601400-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|PIRSR:PIRSR601400-1}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..122
FT                   /note="Somatotropin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014459989"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601400-1"
SQ   SEQUENCE   122 AA;  14184 MW;  0E5B1061E45C8111 CRC64;
     MAAGSWTSLL LAFALLCLPW LQQAGRVPSV PLSRLFDNAM IHAYRLHRLA FDTYQEFRLE
     DGSPRTGQIF KQTYSKFDTN SHNDDTLLKN YWLLHCFRKD MNKVETFLRM VQCRSVEGSC
     GF
//