GAPR1_HUMAN
ID GAPR1_HUMAN Reviewed; 154 AA.
AC Q9H4G4; Q5VZR1; Q8N2S6; Q8WWC9; Q8WX36;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Golgi-associated plant pathogenesis-related protein 1;
DE Short=GAPR-1;
DE Short=Golgi-associated PR-1 protein;
DE AltName: Full=Glioma pathogenesis-related protein 2;
DE Short=GliPR 2;
GN Name=GLIPR2; Synonyms=C9orf19, GAPR1;
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], PROTEIN SEQUENCE OF 35-49 AND 54-68,
RP SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, AND INTERACTION WITH CAV1.
RC TISSUE=Brain;
RX PubMed=11865038; DOI=10.1242/jcs.115.4.827;
RA Eberle H.B., Serrano R.L., Fuellekrug J., Schlosser A., Lehmann W.D.,
RA Lottspeich F., Kaloyanova D., Wieland F.T., Helms J.B.;
RT "Identification and characterization of a novel human plant pathogenesis-
RT related protein that localizes to lipid-enriched microdomains in the Golgi
RT complex.";
RL J. Cell Sci. 115:827-838(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=12137952; DOI=10.1016/s0378-1119(02)00703-5;
RA Eisenberg I., Barash M., Kahan T., Mitrani-Rosenbaum S.;
RT "Cloning and characterization of a human novel gene C9orf19 encoding a
RT conserved putative protein with an SCP-like extracellular protein domain.";
RL Gene 293:141-148(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-90.
RC TISSUE=Prostate;
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).
RN [6]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), AND HOMODIMERIZATION.
RX PubMed=15123429; DOI=10.1016/j.jmb.2004.03.015;
RA Serrano R.L., Kuhn A., Hendricks A., Helms J.B., Sinning I., Groves M.R.;
RT "Structural analysis of the human Golgi-associated plant pathogenesis
RT related protein GAPR-1 implicates dimerization as a regulatory mechanism.";
RL J. Mol. Biol. 339:173-183(2004).
CC -!- SUBUNIT: Homodimer. Interacts with CAV1. {ECO:0000269|PubMed:11865038}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11865038}; Lipid-anchor
CC {ECO:0000269|PubMed:11865038}. Note=Binds lipid-enriched microdomains
CC of Golgi membranes not only by ionic interactions but also through the
CC myristate.
CC -!- TISSUE SPECIFICITY: Highest expression in lung and peripheral
CC leukocytes, and minor expression in liver and kidney.
CC {ECO:0000269|PubMed:12137952}.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; AJ011129; CAC12812.1; -; mRNA.
DR EMBL; AY039756; AAK83460.1; -; mRNA.
DR EMBL; AK074488; BAC11019.1; -; mRNA.
DR EMBL; AK075091; BAC11395.1; -; mRNA.
DR EMBL; AL158830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017918; AAH17918.1; -; mRNA.
DR CCDS; CCDS6598.1; -.
DR RefSeq; NP_071738.1; NM_022343.3.
DR PDB; 1SMB; X-ray; 1.55 A; A=1-154.
DR PDB; 4AIW; X-ray; 1.50 A; A=1-154.
DR PDB; 5VHG; X-ray; 1.27 A; A=4-153.
DR PDBsum; 1SMB; -.
DR PDBsum; 4AIW; -.
DR PDBsum; 5VHG; -.
DR AlphaFoldDB; Q9H4G4; -.
DR SMR; Q9H4G4; -.
DR BioGRID; 127417; 12.
DR DIP; DIP-60127N; -.
DR IntAct; Q9H4G4; 7.
DR MINT; Q9H4G4; -.
DR STRING; 9606.ENSP00000367196; -.
DR DrugBank; DB03661; L-cysteic acid.
DR iPTMnet; Q9H4G4; -.
DR PhosphoSitePlus; Q9H4G4; -.
DR SwissPalm; Q9H4G4; -.
DR BioMuta; GLIPR2; -.
DR EPD; Q9H4G4; -.
DR jPOST; Q9H4G4; -.
DR MassIVE; Q9H4G4; -.
DR MaxQB; Q9H4G4; -.
DR PaxDb; Q9H4G4; -.
DR PeptideAtlas; Q9H4G4; -.
DR PRIDE; Q9H4G4; -.
DR ProteomicsDB; 80836; -.
DR TopDownProteomics; Q9H4G4; -.
DR Antibodypedia; 26141; 165 antibodies from 19 providers.
DR DNASU; 152007; -.
DR Ensembl; ENST00000377960.9; ENSP00000367196.4; ENSG00000122694.16.
DR GeneID; 152007; -.
DR KEGG; hsa:152007; -.
DR MANE-Select; ENST00000377960.9; ENSP00000367196.4; NM_022343.4; NP_071738.1.
DR UCSC; uc003zyz.5; human.
DR CTD; 152007; -.
DR DisGeNET; 152007; -.
DR GeneCards; GLIPR2; -.
DR HGNC; HGNC:18007; GLIPR2.
DR HPA; ENSG00000122694; Low tissue specificity.
DR MIM; 607141; gene.
DR neXtProt; NX_Q9H4G4; -.
DR OpenTargets; ENSG00000122694; -.
DR PharmGKB; PA164720283; -.
DR VEuPathDB; HostDB:ENSG00000122694; -.
DR eggNOG; KOG3017; Eukaryota.
DR GeneTree; ENSGT00390000020276; -.
DR InParanoid; Q9H4G4; -.
DR OMA; NTCAWNK; -.
DR OrthoDB; 1528782at2759; -.
DR PhylomeDB; Q9H4G4; -.
DR TreeFam; TF313138; -.
DR PathwayCommons; Q9H4G4; -.
DR SignaLink; Q9H4G4; -.
DR SIGNOR; Q9H4G4; -.
DR BioGRID-ORCS; 152007; 9 hits in 1085 CRISPR screens.
DR ChiTaRS; GLIPR2; human.
DR EvolutionaryTrace; Q9H4G4; -.
DR GenomeRNAi; 152007; -.
DR Pharos; Q9H4G4; Tbio.
DR PRO; PR:Q9H4G4; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9H4G4; protein.
DR Bgee; ENSG00000122694; Expressed in monocyte and 181 other tissues.
DR ExpressionAtlas; Q9H4G4; baseline and differential.
DR Genevisible; Q9H4G4; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IDA:UniProtKB.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR CDD; cd05382; CAP_GAPR1-like; 1.
DR Gene3D; 3.40.33.10; -; 1.
DR InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR InterPro; IPR014044; CAP_domain.
DR InterPro; IPR035940; CAP_sf.
DR InterPro; IPR001283; CRISP-related.
DR InterPro; IPR034113; SCP_GAPR1-like.
DR PANTHER; PTHR10334; PTHR10334; 1.
DR Pfam; PF00188; CAP; 1.
DR PRINTS; PR00837; V5TPXLIKE.
DR SMART; SM00198; SCP; 1.
DR SUPFAM; SSF55797; SSF55797; 1.
DR PROSITE; PS01009; CRISP_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Direct protein sequencing; Golgi apparatus;
KW Lipoprotein; Membrane; Myristate; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..154
FT /note="Golgi-associated plant pathogenesis-related protein
FT 1"
FT /id="PRO_0000211524"
FT DOMAIN 14..132
FT /note="SCP"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..98
FT /note="Interaction with CAV1"
FT /evidence="ECO:0000269|PubMed:11865038"
FT COILED 30..53
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:11865038,
FT ECO:0000269|PubMed:25255805"
FT CONFLICT 37
FT /note="R -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 87..90
FT /note="IKNY -> VHFM (in Ref. 5; AAH17918)"
FT /evidence="ECO:0000305"
FT CONFLICT 101..154
FT /note="TGHFTAMVWKNTKKMGVGKASASDGSSFVVARYFPAGNVVNEGFFEENVLPP
FT KK -> IRFFFFNFLLFLSKPLLYFSYF (in Ref. 3; BAC11019)"
FT /evidence="ECO:0000305"
FT HELIX 5..23
FT /evidence="ECO:0007829|PDB:5VHG"
FT HELIX 33..49
FT /evidence="ECO:0007829|PDB:5VHG"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5VHG"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:5VHG"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:5VHG"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:5VHG"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:5VHG"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:5VHG"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:5VHG"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:5VHG"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:5VHG"
SQ SEQUENCE 154 AA; 17218 MW; 5AA9B26A21EF1039 CRC64;
MGKSASKQFH NEVLKAHNEY RQKHGVPPLK LCKNLNREAQ QYSEALASTR ILKHSPESSR
GQCGENLAWA SYDQTGKEVA DRWYSEIKNY NFQQPGFTSG TGHFTAMVWK NTKKMGVGKA
SASDGSSFVV ARYFPAGNVV NEGFFEENVL PPKK
