ID RAB44_HUMAN Reviewed; 1021 AA.
AC Q7Z6P3; A0A087WXI0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 4.
DT 24-JAN-2024, entry version 133.
DE RecName: Full=Ras-related protein Rab-44;
GN Name=RAB44;
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2]
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).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; Z85996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS75442.1; -.
DR RefSeq; NP_001244286.1; NM_001257357.1.
DR AlphaFoldDB; Q7Z6P3; -.
DR SMR; Q7Z6P3; -.
DR IntAct; Q7Z6P3; 1.
DR STRING; 9606.ENSP00000481054; -.
DR iPTMnet; Q7Z6P3; -.
DR PhosphoSitePlus; Q7Z6P3; -.
DR BioMuta; RAB44; -.
DR DMDM; 317373517; -.
DR EPD; Q7Z6P3; -.
DR jPOST; Q7Z6P3; -.
DR MassIVE; Q7Z6P3; -.
DR PaxDb; 9606-ENSP00000481054; -.
DR PeptideAtlas; Q7Z6P3; -.
DR ProteomicsDB; 69451; -.
DR TopDownProteomics; Q7Z6P3; -.
DR Antibodypedia; 82285; 2 antibodies from 2 providers.
DR DNASU; 401258; -.
DR Ensembl; ENST00000612677.6; ENSP00000481054.1; ENSG00000255587.9.
DR GeneID; 401258; -.
DR KEGG; hsa:401258; -.
DR MANE-Select; ENST00000612677.6; ENSP00000481054.1; NM_001257357.2; NP_001244286.1.
DR UCSC; uc063oev.1; human.
DR AGR; HGNC:21068; -.
DR CTD; 401258; -.
DR GeneCards; RAB44; -.
DR HGNC; HGNC:21068; RAB44.
DR HPA; ENSG00000255587; Tissue enriched (bone).
DR neXtProt; NX_Q7Z6P3; -.
DR OpenTargets; ENSG00000255587; -.
DR VEuPathDB; HostDB:ENSG00000255587; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000160379; -.
DR HOGENOM; CLU_012405_0_0_1; -.
DR InParanoid; Q7Z6P3; -.
DR OMA; SEMIFDW; -.
DR OrthoDB; 5310663at2759; -.
DR PhylomeDB; Q7Z6P3; -.
DR TreeFam; TF313199; -.
DR PathwayCommons; Q7Z6P3; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q7Z6P3; -.
DR BioGRID-ORCS; 401258; 13 hits in 295 CRISPR screens.
DR GenomeRNAi; 401258; -.
DR Pharos; Q7Z6P3; Tdark.
DR PRO; PR:Q7Z6P3; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q7Z6P3; Protein.
DR Bgee; ENSG00000255587; Expressed in bone marrow and 54 other cell types or tissues.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0002553; P:histamine secretion by mast cell; IEA:Ensembl.
DR GO; GO:0097279; P:histamine secretion mediated by IgE immunoglobulin; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd00154; Rab; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
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; PTHR47977; RAS-RELATED PROTEIN RAB; 1.
DR PANTHER; PTHR47977:SF72; RAS-RELATED PROTEIN RAB-44; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..1021
FT /note="Ras-related protein Rab-44"
FT /id="PRO_0000333077"
FT DOMAIN 77..112
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 191..315
FT /evidence="ECO:0000255"
FT COMPBIAS 445..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..513
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 840..847
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 888..892
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 946..949
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 1019
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 1020
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1021 AA; 110850 MW; 4F8355403845345D CRC64;
METGQRTSRK VRKLGSNRRR QTREPADGEG AAVAPEPESW SSQAAAELQA FFQDCGAKER
GFVTREDLAV AKFSFLGSKE ESEMIFDWVD VERKGHLSLE EFSSGLKNIF GSSQSPHRLR
RRKPLPSKRV SATTSFPALE EADAEEKEAF LAFMEQLGTG HLLPKQMEIW QLWGQLRQEE
PQLAGNLAGF LAKMTSRLQE AQADKEALEL TLRKRDSDHH REVQQLYEEM EQQIRQEKQQ
LQAESDSRGL ALTSQMQDVL EAKEREVQRL AEGQRELEAQ LSHLRSTHQE AASENQQLQE
AKRDLAGRLE EVRGQLQVTR GRLDAARGRV SWQVEEKLSF PGAGEKTPDP QAASPEEAPL
PGLFGDNDDW DQLLSNFGSP PHGALQLCWS PPPTPRATSG PQTPRVVRQI SISEPQAFLF
GQEPSSDPDG APRTPPGVTF SAKDNKGVDP HEQDIRAEQP VEPHDPDPNQ EPGSTPEGRL
LWGLSGSLVA PAFKVLIPLE DGPPPPANSP PPQAPAGSSK QIQASDPDDK GPGSWAPPSG
AQPGAGAGPQ EPTQTPPTMT ERETQPGPSP TTALTGVGPA KPPRQRDALQ QDLHATGSEP
RLGTQRARAL TLGPAEPFQG LEFVGPVPTE RLEQGQAGPA VQEGLPEGLR EAHGQVLGLG
ELSAFPHQEL EEEPRSEEGK QEGRGGQDLS SEQSEQSVEA HGLETAHSEL PQQDSLLVSL
PSATPQAQVE AEGPTPGKSA PPRGSPPRGA QPGAGAGPQE PTQTPPTMAE QEAQPRPSLT
TAHAEEQGPP HSREPRAESR LEDPGMDSRE AGLTPSPGDP MAGGGPQANP DYLFHVIFLG
DSNVGKTSFL HLLHQNSFAT GLTATVGVDF RVKTLLVDNK CFVLQLWDTA GQERYHSMTR
QLLRKADGVV LMYDITSQES FAHVRYWLDC LQDAGSDGVV ILLLGNKMDC EEERQVSVEA
GQQLAQELGV YFGECSAALG HNILEPVVNL ARSLRMQEEG LKDSLVKVAP KRPPKRFGCC
S
//
