ID   GALA_HUMAN              Reviewed;         123 AA.
AC   P22466; Q14413;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   11-NOV-2015, entry version 147.
DE   RecName: Full=Galanin peptides;
DE   Contains:
DE     RecName: Full=Galanin;
DE   Contains:
DE     RecName: Full=Galanin message-associated peptide;
DE              Short=GMAP;
DE   Flags: Precursor;
GN   Name=GAL; Synonyms=GAL1, GALN, GLNN;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RC   TISSUE=Blood;
RX   PubMed=7508413;
RA   Evans H., Baumgartner M., Shine J., Herzog H.;
RT   "Genomic organization and localization of the gene encoding human
RT   preprogalanin.";
RL   Genomics 18:473-477(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 16-123.
RX   PubMed=1370155; DOI=10.2337/diab.41.1.82;
RA   McKnight G.L., Karlsen A.E., Kowalyk S., Mathewes S.L., Sheppard P.O.,
RA   O'Hara P.J., Taborsky G.L.;
RT   "Sequence of human galanin and its inhibition of glucose-stimulated
RT   insulin secretion from RIN cells.";
RL   Diabetes 41:82-87(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cervix;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 33-62.
RX   PubMed=1710578; DOI=10.1016/0014-5793(91)80585-Q;
RA   Bersani M., Johnsen A.H., Hoejrup P., Dunning B.E., Andreasen J.J.,
RA   Holst J.J.;
RT   "Human galanin: primary structure and identification of two molecular
RT   forms.";
RL   FEBS Lett. 283:189-194(1991).
RN   [5]
RP   PROTEIN SEQUENCE OF 33-62, AND SYNTHESIS.
RC   TISSUE=Pituitary;
RX   PubMed=1722333; DOI=10.1073/pnas.88.24.11435;
RA   Schmidt W.E., Kratzin H., Eckart K., Drevs D., Mundkowski G.,
RA   Clemens A., Katsoulis S., Schaefer H., Gallwitz B., Creutzfeldt W.;
RT   "Isolation and primary structure of pituitary human galanin, a 30-
RT   residue nonamidated neuropeptide.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:11435-11439(1991).
RN   [6]
RP   PHOSPHORYLATION AT SER-117.
RC   TISSUE=Pituitary;
RX   PubMed=14997482; DOI=10.1002/pmic.200300584;
RA   Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.;
RT   "Identification and characterization of phosphorylated proteins in the
RT   human pituitary.";
RL   Proteomics 4:587-598(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pituitary;
RX   PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA   Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT   "Phosphoproteomic analysis of the human pituitary.";
RL   Pituitary 9:109-120(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Contracts smooth muscle of the gastrointestinal and
CC       genitourinary tract, regulates growth hormone release, modulates
CC       insulin release, and may be involved in the control of adrenal
CC       secretion.
CC   -!- INTERACTION:
CC       P47211:GALR1; NbExp=2; IntAct=EBI-6624800, EBI-6624741;
CC       O43603:GALR2; NbExp=2; IntAct=EBI-6624800, EBI-6624855;
CC       O43765:SGTA; NbExp=3; IntAct=EBI-6624768, EBI-347996;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the galanin family. {ECO:0000305}.
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DR   EMBL; L11144; AAA18248.1; -; Genomic_DNA.
DR   EMBL; M77140; AAA60178.1; -; mRNA.
DR   EMBL; BC030241; AAH30241.1; -; mRNA.
DR   CCDS; CCDS8183.1; -.
DR   PIR; A49353; RHHUN.
DR   RefSeq; NP_057057.2; NM_015973.4.
DR   UniGene; Hs.278959; -.
DR   ProteinModelPortal; P22466; -.
DR   BioGrid; 119273; 7.
DR   IntAct; P22466; 4.
DR   MINT; MINT-7232142; -.
DR   STRING; 9606.ENSP00000265643; -.
DR   BindingDB; P22466; -.
DR   PhosphoSite; P22466; -.
DR   BioMuta; GAL; -.
DR   DMDM; 2506449; -.
DR   MaxQB; P22466; -.
DR   PaxDb; P22466; -.
DR   PRIDE; P22466; -.
DR   DNASU; 51083; -.
DR   Ensembl; ENST00000265643; ENSP00000265643; ENSG00000069482.
DR   GeneID; 51083; -.
DR   KEGG; hsa:51083; -.
DR   UCSC; uc001oob.3; human.
DR   CTD; 51083; -.
DR   GeneCards; GAL; -.
DR   HGNC; HGNC:4114; GAL.
DR   HPA; CAB000462; -.
DR   HPA; HPA049864; -.
DR   MIM; 137035; gene.
DR   neXtProt; NX_P22466; -.
DR   PharmGKB; PA28529; -.
DR   eggNOG; ENOG410IZPR; Eukaryota.
DR   eggNOG; ENOG410YNUP; LUCA.
DR   GeneTree; ENSGT00390000009663; -.
DR   HOGENOM; HOG000112690; -.
DR   HOVERGEN; HBG005799; -.
DR   InParanoid; P22466; -.
DR   KO; K05244; -.
DR   OMA; WSPAKEK; -.
DR   OrthoDB; EOG79SF01; -.
DR   PhylomeDB; P22466; -.
DR   TreeFam; TF335850; -.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   ChiTaRS; GAL; human.
DR   GeneWiki; Galanin; -.
DR   GenomeRNAi; 51083; -.
DR   NextBio; 53733; -.
DR   PRO; PR:P22466; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; P22466; -.
DR   CleanEx; HS_GAL; -.
DR   Genevisible; P22466; HS.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR   GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IDA:UniProtKB.
DR   GO; GO:0031764; F:type 1 galanin receptor binding; IDA:UniProtKB.
DR   GO; GO:0031765; F:type 2 galanin receptor binding; IDA:UniProtKB.
DR   GO; GO:0031766; F:type 3 galanin receptor binding; IDA:UniProtKB.
DR   GO; GO:0019933; P:cAMP-mediated signaling; IDA:UniProtKB.
DR   GO; GO:0007631; P:feeding behavior; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0030073; P:insulin secretion; NAS:UniProtKB.
DR   GO; GO:0050672; P:negative regulation of lymphocyte proliferation; IEA:Ensembl.
DR   GO; GO:1902891; P:negative regulation of root hair elongation; IDA:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0051795; P:positive regulation of catagen; IDA:UniProtKB.
DR   GO; GO:0051464; P:positive regulation of cortisol secretion; IDA:UniProtKB.
DR   GO; GO:1902608; P:positive regulation of large conductance calcium-activated potassium channel activity; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0010737; P:protein kinase A signaling; IDA:UniProtKB.
DR   GO; GO:0031943; P:regulation of glucocorticoid metabolic process; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR   GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR   GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR   InterPro; IPR008174; Galanin.
DR   InterPro; IPR008175; Galanin_pre.
DR   InterPro; IPR013068; GMAP.
DR   Pfam; PF01296; Galanin; 1.
DR   Pfam; PF06540; GMAP; 1.
DR   PRINTS; PR00273; GALANIN.
DR   ProDom; PD005962; Galanin; 1.
DR   ProDom; PD012185; GMAP; 1.
DR   SMART; SM00071; Galanin; 1.
DR   PROSITE; PS00861; GALANIN; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Hormone; Neuropeptide; Phosphoprotein;
KW   Polymorphism; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   PROPEP       20     30
FT                                /FTId=PRO_0000010448.
FT   PEPTIDE      33     62       Galanin.
FT                                /FTId=PRO_0000010449.
FT   PEPTIDE      65    123       Galanin message-associated peptide.
FT                                /FTId=PRO_0000010450.
FT   MOD_RES     117    117       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692,
FT                                ECO:0000269|PubMed:14997482}.
FT   VARIANT      16     16       A -> V (in dbSNP:rs34725707).
FT                                /FTId=VAR_049121.
SQ   SEQUENCE   123 AA;  13302 MW;  48D2170AF1248E6D CRC64;
     MARGSALLLA SLLLAAALSA SAGLWSPAKE KRGWTLNSAG YLLGPHAVGN HRSFSDKNGL
     TSKRELRPED DMKPGSFDRS IPENNIMRTI IEFLSFLHLK EAGALDRLLD LPAAASSEDI
     ERS
//