LOCUS       NP_001395248            1955 aa            linear   ROD 02-MAY-2024
DEFINITION  rho GTPase-activating protein 21 isoform 1 [Mus musculus].
ACCESSION   NP_001395248 XP_006497606
VERSION     NP_001395248.1
DBSOURCE    REFSEQ: accession NM_001408319.1
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1955)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1955)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1955)
  AUTHORS   Bernusso,V.A., Vieira,K.P., Duarte,A.S.S., Lescano,C.H.,
            Monica,F.Z., Vicente,C.P., De Paula,E.V., Saad,S.T.O. and
            Lazarini,M.
  TITLE     Deficiency of ARHGAP21 alters megakaryocytic cell lineage responses
            and enhances platelet hemostatic function
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1868 (6), 119012 (2021)
   PUBMED   33727037
  REMARK    GeneRIF: Deficiency of ARHGAP21 alters megakaryocytic cell lineage
            responses and enhances platelet hemostatic function.
REFERENCE   4  (residues 1 to 1955)
  AUTHORS   Ferreira,S.M., Costa-Junior,J.M., Kurauti,M.A., Leite,N.C.,
            Ortis,F., Rezende,L.F., Barbosa,H.C., Boschero,A.C. and Santos,G.J.
  TITLE     ARHGAP21 Acts as an Inhibitor of the Glucose-Stimulated Insulin
            Secretion Process
  JOURNAL   Front Endocrinol (Lausanne) 11, 599165 (2020)
   PUBMED   33324349
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1955)
  AUTHORS   Zangerolamo,L., Soares,G.M., Vettorazzi,J.F., do Amaral,M.E.,
            Carneiro,E.M., Olalla-Saad,S.T., Boschero,A.C. and
            Barbosa-Sampaio,H.C.
  TITLE     ARHGAP21 deficiency impairs hepatic lipid metabolism and improves
            insulin signaling in lean and obese mice
  JOURNAL   Can J Physiol Pharmacol 97 (11), 1018-1027 (2019)
   PUBMED   31247150
  REMARK    GeneRIF: liver of ARHGAP21-haplodeficient mice are more insulin
            sensitive, associated with higher lipid synthesis and lower lipid
            export
REFERENCE   6  (residues 1 to 1955)
  AUTHORS   Menetrey,J., Perderiset,M., Cicolari,J., Dubois,T., Elkhatib,N., El
            Khadali,F., Franco,M., Chavrier,P. and Houdusse,A.
  TITLE     Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi
            membranes
  JOURNAL   EMBO J 26 (7), 1953-1962 (2007)
   PUBMED   17347647
REFERENCE   7  (residues 1 to 1955)
  AUTHORS   Nishimura,M., Yokoi,N., Miki,T., Horikawa,Y., Yoshioka,H.,
            Takeda,J., Ohara,O. and Seino,S.
  TITLE     Construction of a multi-functional cDNA library specific for mouse
            pancreatic islets and its application to microarray
  JOURNAL   DNA Res 11 (5), 315-323 (2004)
   PUBMED   15747579
REFERENCE   8  (residues 1 to 1955)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Aizawa,H., Yuasa,S.,
            Nakajima,D., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: II. The complete nucleotide sequences of 400 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (1), 35-48 (2003)
   PUBMED   12693553
REFERENCE   9  (residues 1 to 1955)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   10 (residues 1 to 1955)
  AUTHORS   Piao,Y., Ko,N.T., Lim,M.K. and Ko,M.S.
  TITLE     Construction of long-transcript enriched cDNA libraries from
            submicrogram amounts of total RNAs by a universal PCR amplification
            method
  JOURNAL   Genome Res 11 (9), 1553-1558 (2001)
   PUBMED   11544199
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL773540.18, BX649226.1 and AL929100.11.
            
            On Jun 15, 2022 this sequence version replaced XP_006497606.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR10223969.1488.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164138, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1955
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 14.6 cM"
     Protein         1..1955
                     /product="rho GTPase-activating protein 21 isoform 1"
                     /note="rho GTPase-activating protein 21; rho
                     GTPase-activating protein 10; rho-type GTPase-activating
                     protein 21"
                     /calculated_mol_wt=216851
     Region          26..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          54..162
                     /region_name="PDZ_ARHGAP21_23-like"
                     /note="PDZ domain of ARHGAP21 and ARHGAP23, and related
                     domains; cd06756"
                     /db_xref="CDD:467238"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T5U3; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            order(65..71,111,114,143,147,150..151)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467238"
     Region          220..239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          336..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T5U3; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          509..529
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            559
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q5T5U3; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            579
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          583..657
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            620
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T5U3; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            629
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T5U3; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          684..712
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            751
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5T5U3; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            861
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          862..889
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            866
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            885
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T5U3; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q5T5U3; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          912..931
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            928
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            930
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          934..1101
                     /region_name="Interaction with ARF1 and ARF6.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          937..1046
                     /region_name="PH_ARHGAP21-like"
                     /note="ARHGAP21 and related proteins pleckstrin homology
                     (PH) domain; cd01253"
                     /db_xref="CDD:269955"
     Site            order(937..954,959..985,987..1019,1021..1044)
                     /site_type="other"
                     /note="ARF1 binding site [polypeptide binding]"
                     /db_xref="CDD:269955"
     Site            958
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T5U3; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          1090..1130
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            1103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16452087; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            1119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T5U3; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          1148..1343
                     /region_name="RhoGAP_ARHGAP21"
                     /note="RhoGAP (GTPase-activator protein [GAP] for Rho-like
                     small GTPases) domain of ArhGAP21-like proteins. ArhGAP21
                     is a multi-domain protein, containing RhoGAP, PH and PDZ
                     domains, and is believed to play a role in the
                     organization of the cell-cell junction...; cd04395"
                     /db_xref="CDD:239860"
     Site            order(1188,1228,1232,1301,1304..1305,1329)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239860"
     Site            1188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239860"
     Region          1383..1406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          1422..1642
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            1422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T5U3; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            1436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T5U3; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            1437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            1514
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5T5U3; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          1589..1858
                     /region_name="Interaction with CTNNA1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          1659..1804
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            1666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            1679
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            1739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T5U3; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Region          1856..1955
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            1912
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     Site            1916
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6DFV3.2)"
     CDS             1..1955
                     /gene="Arhgap21"
                     /gene_synonym="5530401C11Rik; ARHGAP10"
                     /coded_by="NM_001408319.1:433..6300"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:71435"
                     /db_xref="MGI:MGI:1918685"
ORIGIN      
        1 mmathwtglp eedgdklkac gaasacevsk nkdgkdqgep vspsedepfs wpgpktvmlk
       61 rtsqgfgftl rhfivyppes aiqfsykdee ngnrggkqrn rlepmdtifv kqvkeggpaf
      121 eaglctgdri ikvngesvig ktysqviali qnsdttlels vmpkdedilq vlqftkdvta
      181 laysqdaylk gneaysgnar nipepppvcy pwlpstpsat aqpvetcppd slpnkqqtsa
      241 pvltqpgray rmeiqvppsp tdvaksntav cvcnesvrtv ivpsekvvdl lanrnnpsgp
      301 shrteevryg vneqastkaa srttspasvp tahlihqttg srslepsgil lksgnysghs
      361 egisssrsqa vdsppvsvnh ysanshqhid wknyktykey idnrrlhigc rtiqerldsl
      421 raasqsaady nqvvptrttl qvrrrstshd rvpqsvqirq rsvsqerled svlmkycprs
      481 asqgaltspp vsfnnhrtrs wdyiegqtea tatvnsesqi pdsngerkqt ykwsgfteqd
      541 drrgiherpr qqemhkpfrg snltvapvvn sdnrrlvgrg vgpvsqfkki ppdlrpphsn
      601 rnfptttgvs lqrgiaqdrs plvkvrsnsl kvppppvskp sfsqhslasm kdqrpvnhlh
      661 qhsvlsqqtq frsestfehq letevssclp gtsaktspql senlgtsdle lpaiprngdi
      721 nlqeaeiqqp dvldnkesvi lrekpqsgrq tpqplrhqsy ilavndqetg sdttcwlpnd
      781 arrevhikrm eerkasstsp pgdslasipf ideptspsid heiahipasa visastahvp
      841 siatvppslt tsaplirrql shdqesvgpp sldgqhsskt ersksydegl ddyredakls
      901 fkhvsslkgi kitdsqksse dsgsrkgsss evfsdaareg wlqfrplvtd kgkrvggsir
      961 pwkqmyvvlr ghslylykdr reqttpseee qpisvnacli disysetkrr nvfrlttsdc
     1021 eclfqaedrd dmlswiktiq essnlneedt gvtnrdlisr rikeynslls kteqlpktpr
     1081 qslsirqtll gaksepktqs phspkeeser kllskddtsp pkdkgtwrrg ipsivrktfe
     1141 kkpaatgtfg vrlddcppah tnryiplivd iccklveerg leytgiyrvp gnnaaissmq
     1201 eelnkgmadi diqddkwrdl nvissllksf frklpeplft ndkyadfiea nrkedpldrl
     1261 rtlkrlihdl pehhfetlkf lsahlktvae nseknkmepr nlaivfgptl vrtsednmth
     1321 mvthmpdqyk ivetliqhhd wffteegaee pltavqeent vdsqpvpnid hlltnigrtg
     1381 vlpgdvsdsa tsdsakskgs wgsgkdqysr ellvssifaa asrkrkkpke kaqpsssede
     1441 ldsvffkken teqshseike eskresetsg skqrvvvake sntkkdsgtt keekkipwee
     1501 pspphsskrn rsptlscrla mlkegprsll tqkphceetg sdsgtllsts sqasllrsst
     1561 kkstspetkh seflsiagtt tsdysttsst tyltsldssr lspevqsvae skgdeadder
     1621 selvsegrpv etdsesefpv fpttltsdrl frgkfqevar vsrrnsegse asctegsltp
     1681 sldsrrqqfs shrliecdtl srkksarfks dsgspgdtrt eketpalakm fdvmkkgkst
     1741 gslltpsrse sekqeatwkt kiadrlklrp rapaddmfgv gnqkptaeta krknikrrht
     1801 lgghrdatei svlsfwkahe qsadkesels avnrlkpkcs aqdlsisdwl arervrtsas
     1861 dlsrgeglep qaespsvlgt pisthsppsq qpearvaats tlastsqspl ftppqspdqi
     1921 nresfqnmsq nasstanihp hkqsespdtk aetpp
//
