ID   REM1_HUMAN              Reviewed;         298 AA.
AC   O75628; E1P5L1; Q5TZR7; Q5TZR8; Q9NP57;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2003, sequence version 2.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=GTP-binding protein REM 1;
DE   AltName: Full=GTPase-regulating endothelial cell sprouting;
DE   AltName: Full=Rad and Gem-like GTP-binding protein 1;
GN   Name=REM1; Synonyms=GES, REM;
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].
RA   Finlin B.S., Andres D.A.;
RT   "Cloning of the human Rem gene.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF THR-94.
RC   TISSUE=Lymph node;
RX   PubMed=10831614; DOI=10.1083/jcb.149.5.1107;
RA   Pan J.Y., Fieles W.E., White A.M., Egerton M.M., Silberstein D.S.;
RT   "Ges, a human GTPase of the Rad/Gem/Kir family, promotes endothelial cell
RT   sprouting and cytoskeleton reorganization.";
RL   J. Cell Biol. 149:1107-1116(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-28.
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-28.
RC   TISSUE=Caudate nucleus;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: Promotes endothelial cell sprouting and actin cytoskeletal
CC       reorganization. May be involved in angiogenesis. May function in Ca(2+)
CC       signaling.
CC   -!- SUBUNIT: In vitro, interacts with calmodulin in a calcium-dependent
CC       manner.
CC   -!- TISSUE SPECIFICITY: Most highly expressed in the endothelial lining of
CC       the blood vessels in uterus and heart. Lower levels found in spleen,
CC       lymph node, kidney and testis. Also found in cells with secretory
CC       function such as the islets of Langerhans, lobule/duct epithelium in
CC       the breast, bile duct epithelium in the liver, surface epithelium in
CC       the endometrial glands of the uterus, colon mucosa and acinar cells in
CC       the pancreas and the prostate.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. RGK family.
CC       {ECO:0000305}.
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DR   EMBL; AF084465; AAC33132.1; -; mRNA.
DR   EMBL; AF152863; AAF74212.1; -; mRNA.
DR   EMBL; BT020078; AAV38881.1; -; mRNA.
DR   EMBL; BT020079; AAV38882.1; -; mRNA.
DR   EMBL; AK313060; BAG35890.1; -; mRNA.
DR   EMBL; AL121751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW76439.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76440.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76442.1; -; Genomic_DNA.
DR   EMBL; BC039813; AAH39813.1; -; mRNA.
DR   CCDS; CCDS13181.1; -.
DR   RefSeq; NP_054731.2; NM_014012.5.
DR   PDB; 2NZJ; X-ray; 2.50 A; A/B/C/D=79-251.
DR   PDBsum; 2NZJ; -.
DR   AlphaFoldDB; O75628; -.
DR   SMR; O75628; -.
DR   BioGRID; 118781; 8.
DR   STRING; 9606.ENSP00000201979; -.
DR   GlyGen; O75628; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; O75628; -.
DR   PhosphoSitePlus; O75628; -.
DR   BioMuta; REM1; -.
DR   jPOST; O75628; -.
DR   MassIVE; O75628; -.
DR   PaxDb; 9606-ENSP00000201979; -.
DR   PeptideAtlas; O75628; -.
DR   ProteomicsDB; 50127; -.
DR   Antibodypedia; 10156; 117 antibodies from 27 providers.
DR   DNASU; 28954; -.
DR   Ensembl; ENST00000201979.3; ENSP00000201979.2; ENSG00000088320.4.
DR   GeneID; 28954; -.
DR   KEGG; hsa:28954; -.
DR   MANE-Select; ENST00000201979.3; ENSP00000201979.2; NM_014012.6; NP_054731.2.
DR   UCSC; uc002wwa.5; human.
DR   AGR; HGNC:15922; -.
DR   CTD; 28954; -.
DR   DisGeNET; 28954; -.
DR   GeneCards; REM1; -.
DR   HGNC; HGNC:15922; REM1.
DR   HPA; ENSG00000088320; Tissue enhanced (cervix).
DR   MIM; 610388; gene.
DR   neXtProt; NX_O75628; -.
DR   OpenTargets; ENSG00000088320; -.
DR   PharmGKB; PA34324; -.
DR   VEuPathDB; HostDB:ENSG00000088320; -.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000160613; -.
DR   HOGENOM; CLU_041217_3_2_1; -.
DR   InParanoid; O75628; -.
DR   OMA; DCLYHVV; -.
DR   OrthoDB; 5473132at2759; -.
DR   PhylomeDB; O75628; -.
DR   TreeFam; TF314379; -.
DR   PathwayCommons; O75628; -.
DR   SignaLink; O75628; -.
DR   SIGNOR; O75628; -.
DR   BioGRID-ORCS; 28954; 22 hits in 1146 CRISPR screens.
DR   EvolutionaryTrace; O75628; -.
DR   GenomeRNAi; 28954; -.
DR   Pharos; O75628; Tbio.
DR   PRO; PR:O75628; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; O75628; Protein.
DR   Bgee; ENSG00000088320; Expressed in endocervix and 154 other cell types or tissues.
DR   GO; GO:0031674; C:I band; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR   GO; GO:0005246; F:calcium channel regulator activity; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR   GO; GO:1904878; P:negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IEA:Ensembl.
DR   GO; GO:0014722; P:regulation of skeletal muscle contraction by calcium ion signaling; IEA:Ensembl.
DR   CDD; cd04148; RGK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR017358; RGK.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR45775:SF2; GTP-BINDING PROTEIN REM 1; 1.
DR   PANTHER; PTHR45775; RAD, GEM/KIR FAMILY MEMBER 2, ISOFORM C; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PIRSF; PIRSF038017; GTP-binding_GEM; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51421; RAS; 1.
DR   Genevisible; O75628; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Calmodulin-binding; GTP-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..298
FT                   /note="GTP-binding protein REM 1"
FT                   /id="PRO_0000122481"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..287
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        31..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87..94
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         195..198
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35929"
FT   VARIANT         28
FT                   /note="H -> R (in dbSNP:rs1006459)"
FT                   /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3"
FT                   /id="VAR_049498"
FT   VARIANT         45
FT                   /note="R -> W (in dbSNP:rs59730832)"
FT                   /id="VAR_061232"
FT   VARIANT         59
FT                   /note="P -> A (in dbSNP:rs2233829)"
FT                   /id="VAR_049499"
FT   MUTAGEN         94
FT                   /note="T->N: No endothelial cell sprouting."
FT                   /evidence="ECO:0000269|PubMed:10831614"
FT   CONFLICT        209
FT                   /note="E -> V (in Ref. 1; AAC33132)"
FT                   /evidence="ECO:0000305"
FT   STRAND          80..86
FT                   /evidence="ECO:0007829|PDB:2NZJ"
FT   HELIX           93..101
FT                   /evidence="ECO:0007829|PDB:2NZJ"
FT   STRAND          112..123
FT                   /evidence="ECO:0007829|PDB:2NZJ"
FT   STRAND          126..133
FT                   /evidence="ECO:0007829|PDB:2NZJ"
FT   HELIX           145..149
FT                   /evidence="ECO:0007829|PDB:2NZJ"
FT   TURN            150..152
FT                   /evidence="ECO:0007829|PDB:2NZJ"
FT   STRAND          155..162
FT                   /evidence="ECO:0007829|PDB:2NZJ"
FT   HELIX           166..181
FT                   /evidence="ECO:0007829|PDB:2NZJ"
FT   STRAND          190..195
FT                   /evidence="ECO:0007829|PDB:2NZJ"
FT   TURN            200..202
FT                   /evidence="ECO:0007829|PDB:2NZJ"
FT   HELIX           207..217
FT                   /evidence="ECO:0007829|PDB:2NZJ"
FT   STRAND          219..223
FT                   /evidence="ECO:0007829|PDB:2NZJ"
FT   TURN            226..229
FT                   /evidence="ECO:0007829|PDB:2NZJ"
FT   HELIX           232..247
FT                   /evidence="ECO:0007829|PDB:2NZJ"
SQ   SEQUENCE   298 AA;  32947 MW;  E7CCE776FFD42CD7 CRC64;
     MTLNTEQEAK TPLHRRASTP LPLSPRGHQP GRLSTVPSTQ SQHPRLGQSA SLNPPTQKPS
     PAPDDWSSES SDSEGSWEAL YRVVLLGDPG VGKTSLASLF AGKQERDLHE QLGEDVYERT
     LTVDGEDTTL VVVDTWEAEK LDKSWSQESC LQGGSAYVIV YSIADRGSFE SASELRIQLR
     RTHQADHVPI ILVGNKADLA RCREVSVEEG RACAVVFDCK FIETSATLQH NVAELFEGVV
     RQLRLRRRDS AAKEPPAPRR PASLAQRARR FLARLTARSA RRRALKARSK SCHNLAVL
//