ID   GAS1_HUMAN              Reviewed;         345 AA.
AC   P54826; B9EGM4; Q6B086;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Growth arrest-specific protein 1;
DE            Short=GAS-1;
DE   Flags: Precursor;
GN   Name=GAS1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Liver;
RX   PubMed=8127893; DOI=10.1073/pnas.91.5.1848;
RA   del Sal G., Collavin L., Ruaro M.E., Edomi P., Saccone S., Valle G.D.,
RA   Schneider C.;
RT   "Structure, function, and chromosome mapping of the growth-suppressing
RT   human homologue of the murine gas1 gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:1848-1852(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Specific growth arrest protein involved in growth
CC       suppression. Blocks entry to S phase. Prevents cycling of normal and
CC       transformed cells. Binds 20(S)-hydroxycholesterol (20(S)-OHC) (By
CC       similarity). {ECO:0000250|UniProtKB:Q01721,
CC       ECO:0000269|PubMed:8127893}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
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DR   EMBL; L13698; AAA72368.1; -; mRNA.
DR   EMBL; AL158149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC074908; AAH74908.1; -; mRNA.
DR   EMBL; BC074809; AAH74809.1; -; mRNA.
DR   EMBL; BC132682; AAI32683.1; -; mRNA.
DR   EMBL; BC136586; AAI36587.1; -; mRNA.
DR   CCDS; CCDS6674.1; -.
DR   PIR; A53138; A53138.
DR   RefSeq; NP_002039.2; NM_002048.2.
DR   PDB; 7RHQ; EM; 3.53 A; G=40-317.
DR   PDBsum; 7RHQ; -.
DR   AlphaFoldDB; P54826; -.
DR   EMDB; EMD-24466; -.
DR   SMR; P54826; -.
DR   BioGRID; 108889; 9.
DR   IntAct; P54826; 1.
DR   MINT; P54826; -.
DR   STRING; 9606.ENSP00000298743; -.
DR   GlyCosmos; P54826; 1 site, No reported glycans.
DR   GlyGen; P54826; 1 site.
DR   iPTMnet; P54826; -.
DR   PhosphoSitePlus; P54826; -.
DR   BioMuta; GAS1; -.
DR   DMDM; 218512049; -.
DR   jPOST; P54826; -.
DR   MassIVE; P54826; -.
DR   MaxQB; P54826; -.
DR   PaxDb; 9606-ENSP00000298743; -.
DR   PeptideAtlas; P54826; -.
DR   ProteomicsDB; 56734; -.
DR   Pumba; P54826; -.
DR   Antibodypedia; 13350; 283 antibodies from 31 providers.
DR   DNASU; 2619; -.
DR   Ensembl; ENST00000298743.9; ENSP00000298743.7; ENSG00000180447.7.
DR   GeneID; 2619; -.
DR   KEGG; hsa:2619; -.
DR   MANE-Select; ENST00000298743.9; ENSP00000298743.7; NM_002048.3; NP_002039.2.
DR   UCSC; uc004aox.5; human.
DR   AGR; HGNC:4165; -.
DR   CTD; 2619; -.
DR   DisGeNET; 2619; -.
DR   GeneCards; GAS1; -.
DR   GeneReviews; GAS1; -.
DR   HGNC; HGNC:4165; GAS1.
DR   HPA; ENSG00000180447; Tissue enhanced (endometrium).
DR   MalaCards; GAS1; -.
DR   MIM; 139185; gene.
DR   neXtProt; NX_P54826; -.
DR   OpenTargets; ENSG00000180447; -.
DR   Orphanet; 93925; Alobar holoprosencephaly.
DR   Orphanet; 93924; Lobar holoprosencephaly.
DR   Orphanet; 280200; Microform holoprosencephaly.
DR   Orphanet; 93926; Midline interhemispheric variant of holoprosencephaly.
DR   Orphanet; 220386; Semilobar holoprosencephaly.
DR   Orphanet; 280195; Septopreoptic holoprosencephaly.
DR   PharmGKB; PA28578; -.
DR   VEuPathDB; HostDB:ENSG00000180447; -.
DR   eggNOG; ENOG502QSF7; Eukaryota.
DR   GeneTree; ENSGT00390000001195; -.
DR   HOGENOM; CLU_068697_1_0_1; -.
DR   InParanoid; P54826; -.
DR   OMA; NRYLTYC; -.
DR   OrthoDB; 5323788at2759; -.
DR   PhylomeDB; P54826; -.
DR   TreeFam; TF329660; -.
DR   PathwayCommons; P54826; -.
DR   Reactome; R-HSA-5632681; Ligand-receptor interactions.
DR   Reactome; R-HSA-5635838; Activation of SMO.
DR   SignaLink; P54826; -.
DR   SIGNOR; P54826; -.
DR   BioGRID-ORCS; 2619; 17 hits in 1151 CRISPR screens.
DR   ChiTaRS; GAS1; human.
DR   GeneWiki; GAS1; -.
DR   GenomeRNAi; 2619; -.
DR   Pharos; P54826; Tbio.
DR   PRO; PR:P54826; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; P54826; Protein.
DR   Bgee; ENSG00000180447; Expressed in germinal epithelium of ovary and 197 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008142; F:oxysterol binding; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0045165; P:cell fate commitment; ISS:UniProtKB.
DR   GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IEP:UniProtKB.
DR   GO; GO:0048589; P:developmental growth; ISS:UniProtKB.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:UniProtKB.
DR   GO; GO:0010955; P:negative regulation of protein processing; IMP:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR   GO; GO:0008589; P:regulation of smoothened signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR039596; GAS1.
DR   InterPro; IPR016017; GDNF/GAS1.
DR   PANTHER; PTHR16840; GROWTH ARREST-SPECIFIC PROTEIN 1; 1.
DR   PANTHER; PTHR16840:SF3; GROWTH ARREST-SPECIFIC PROTEIN 1; 1.
DR   Pfam; PF02351; GDNF; 1.
DR   SMART; SM00907; GDNF; 2.
DR   Genevisible; P54826; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell membrane; Glycoprotein; GPI-anchor;
KW   Growth arrest; Lipoprotein; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..318
FT                   /note="Growth arrest-specific protein 1"
FT                   /id="PRO_0000021318"
FT   PROPEP          319..345
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000021319"
FT   REGION          254..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           318
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        216
FT                   /note="A -> V (in Ref. 1; AAA72368)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   345 AA;  35693 MW;  31A0CBEEC3632F82 CRC64;
     MVAALLGGGG EARGGTVPGA WLCLMALLQL LGSAPRGSGL AHGRRLICWQ ALLQCQGEPE
     CSYAYNQYAE ACAPVLAQHG GGDAPGAAAA AFPASAASFS SRWRCPSHCI SALIQLNHTR
     RGPALEDCDC AQDENCKSTK RAIEPCLPRT SGGGAGGPGA GGVMGCTEAR RRCDRDSRCN
     LALSRYLTYC GKVFNGLRCT DECRTVIEDM LAMPKAALLN DCVCDGLERP ICESVKENMA
     RLCFGAELGN GPGSSGSDGG LDDYYDEDYD DEQRTGGAGG EQPLDDDDGV PHPPRPGSGA
     AASGGRGDLP YGPGRRSSGG GGRLAPRGAW TPLASILLLL LGPLF
//