ID   RAB37_HUMAN             Reviewed;         223 AA.
AC   Q96AX2; A8MXF5; A8MYT0; Q8IWA7;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Ras-related protein Rab-37;
DE   Flags: Precursor;
GN   Name=RAB37;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   TISSUE=Thalamus, Thymus, and Trachea;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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   [5]
RP   PROTEIN SEQUENCE OF 2-11, AND ACETYLATION AT THR-2.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
CC   -!- SUBUNIT: Interacts with RIMS1. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q96AX2; Q969L2: MAL2; NbExp=3; IntAct=EBI-748121, EBI-944295;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle. Note=Secretory granules.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q96AX2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96AX2-2; Sequence=VSP_041268;
CC       Name=3;
CC         IsoId=Q96AX2-3; Sequence=VSP_043155;
CC       Name=4;
CC         IsoId=Q96AX2-4; Sequence=VSP_043156;
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AK098068; BAC05227.1; -; mRNA.
DR   EMBL; AK290202; BAF82891.1; -; mRNA.
DR   EMBL; AK296172; BAH12272.1; -; mRNA.
DR   EMBL; AK303442; BAH13962.1; -; mRNA.
DR   EMBL; AC016888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC064805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471099; EAW89180.1; -; Genomic_DNA.
DR   EMBL; BC016615; AAH16615.1; -; mRNA.
DR   EMBL; BC040547; AAH40547.1; -; mRNA.
DR   CCDS; CCDS11703.1; -. [Q96AX2-2]
DR   CCDS; CCDS32722.1; -. [Q96AX2-1]
DR   CCDS; CCDS54162.1; -. [Q96AX2-4]
DR   RefSeq; NP_001006639.1; NM_001006638.2. [Q96AX2-1]
DR   RefSeq; NP_001157461.1; NM_001163989.1.
DR   RefSeq; NP_001157462.1; NM_001163990.1. [Q96AX2-4]
DR   RefSeq; NP_001317400.1; NM_001330471.1.
DR   RefSeq; NP_783865.1; NM_175738.4. [Q96AX2-2]
DR   AlphaFoldDB; Q96AX2; -.
DR   SMR; Q96AX2; -.
DR   BioGRID; 130604; 11.
DR   IntAct; Q96AX2; 5.
DR   STRING; 9606.ENSP00000376390; -.
DR   iPTMnet; Q96AX2; -.
DR   PhosphoSitePlus; Q96AX2; -.
DR   BioMuta; RAB37; -.
DR   DMDM; 20139581; -.
DR   jPOST; Q96AX2; -.
DR   MassIVE; Q96AX2; -.
DR   MaxQB; Q96AX2; -.
DR   PaxDb; 9606-ENSP00000376390; -.
DR   PeptideAtlas; Q96AX2; -.
DR   ProteomicsDB; 76005; -. [Q96AX2-1]
DR   ProteomicsDB; 76006; -. [Q96AX2-2]
DR   ProteomicsDB; 76007; -. [Q96AX2-3]
DR   ProteomicsDB; 76008; -. [Q96AX2-4]
DR   Antibodypedia; 31994; 427 antibodies from 28 providers.
DR   DNASU; 326624; -.
DR   Ensembl; ENST00000392612.7; ENSP00000376388.3; ENSG00000172794.20. [Q96AX2-4]
DR   Ensembl; ENST00000392613.10; ENSP00000376389.5; ENSG00000172794.20. [Q96AX2-1]
DR   Ensembl; ENST00000402449.8; ENSP00000383934.4; ENSG00000172794.20. [Q96AX2-2]
DR   Ensembl; ENST00000481224.5; ENSP00000436563.1; ENSG00000172794.20. [Q96AX2-1]
DR   Ensembl; ENST00000613645.1; ENSP00000483155.1; ENSG00000172794.20. [Q96AX2-1]
DR   GeneID; 326624; -.
DR   KEGG; hsa:326624; -.
DR   MANE-Select; ENST00000392613.10; ENSP00000376389.5; NM_001006638.3; NP_001006639.1.
DR   UCSC; uc002jlk.4; human. [Q96AX2-1]
DR   AGR; HGNC:30268; -.
DR   CTD; 326624; -.
DR   DisGeNET; 326624; -.
DR   GeneCards; RAB37; -.
DR   HGNC; HGNC:30268; RAB37.
DR   HPA; ENSG00000172794; Tissue enhanced (bone marrow, brain, lymphoid tissue).
DR   MIM; 609956; gene.
DR   neXtProt; NX_Q96AX2; -.
DR   OpenTargets; ENSG00000172794; -.
DR   PharmGKB; PA134901093; -.
DR   VEuPathDB; HostDB:ENSG00000172794; -.
DR   eggNOG; KOG0083; Eukaryota.
DR   GeneTree; ENSGT00940000158883; -.
DR   InParanoid; Q96AX2; -.
DR   OMA; ISACYKT; -.
DR   OrthoDB; 8685at2759; -.
DR   PhylomeDB; Q96AX2; -.
DR   TreeFam; TF323428; -.
DR   BRENDA; 3.6.5.2; 2681.
DR   PathwayCommons; Q96AX2; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR   SignaLink; Q96AX2; -.
DR   SIGNOR; Q96AX2; -.
DR   BioGRID-ORCS; 326624; 8 hits in 1144 CRISPR screens.
DR   ChiTaRS; RAB37; human.
DR   GeneWiki; RAB37; -.
DR   GenomeRNAi; 326624; -.
DR   Pharos; Q96AX2; Tbio.
DR   PRO; PR:Q96AX2; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q96AX2; Protein.
DR   Bgee; ENSG00000172794; Expressed in cerebellar hemisphere and 118 other cell types or tissues.
DR   ExpressionAtlas; Q96AX2; baseline and differential.
DR   GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd04112; Rab26; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47978; -; 1.
DR   PANTHER; PTHR47978:SF68; RAS-RELATED PROTEIN RAB-37; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00177; ARF; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   Genevisible; Q96AX2; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasmic vesicle;
KW   Direct protein sequencing; GTP-binding; Lipoprotein; Methylation;
KW   Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12665801"
FT   CHAIN           2..220
FT                   /note="Ras-related protein Rab-37"
FT                   /id="PRO_0000121249"
FT   PROPEP          221..223
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000370828"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           59..67
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         36..43
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         85..89
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         143..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000269|PubMed:12665801"
FT   MOD_RES         220
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           219
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           220
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..68
FT                   /note="MTGTPGAVATRDGEAPERSPPCSPSYDLTGKVMLLGDTGVGKTCFLIQFKDG
FT                   AFLSGTFIATVGIDFR -> MDLQRPDSYQGGAGPDFNDHVLHKTILVGDSGVGKTSLL
FT                   VQFDQGKFIPGSFSATVGIGFT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_041268"
FT   VAR_SEQ         1..30
FT                   /note="MTGTPGAVATRDGEAPERSPPCSPSYDLTG -> MWLMSEAHGAEPVLLREA
FT                   ARPFTQTLRLCVPSGNS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043155"
FT   VAR_SEQ         32..68
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043156"
FT   VARIANT         188
FT                   /note="A -> P (in dbSNP:rs34215331)"
FT                   /id="VAR_034434"
SQ   SEQUENCE   223 AA;  24815 MW;  5A7A4887BCBB84A8 CRC64;
     MTGTPGAVAT RDGEAPERSP PCSPSYDLTG KVMLLGDTGV GKTCFLIQFK DGAFLSGTFI
     ATVGIDFRNK VVTVDGVRVK LQIWDTAGQE RFRSVTHAYY RDAQALLLLY DITNKSSFDN
     IRAWLTEIHE YAQRDVVIML LGNKADMSSE RVIRSEDGET LAREYGVPFL ETSAKTGMNV
     ELAFLAIAKE LKYRAGHQAD EPSFQIRDYV ESQKKRSSCC SFM
//