LOCUS       NP_001343453            1266 aa            linear   ROD 02-MAY-2024
DEFINITION  rho GTPase-activating protein 29 [Mus musculus].
ACCESSION   NP_001343453 XP_006501351
VERSION     NP_001343453.1
DBSOURCE    REFSEQ: accession NM_001356524.1
KEYWORDS    RefSeq; RefSeq Select.
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 1266)
  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 1266)
  AUTHORS   Li,M.J., Shi,J.Y., Zhang,B.H., Chen,Q.M., Shi,B. and Jia,Z.L.
  TITLE     Targeted re-sequencing on 1p22 among non-syndromic orofacial clefts
            from Han Chinese population
  JOURNAL   Front Genet 13, 947126 (2022)
   PUBMED   36061182
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1266)
  AUTHORS   Bertol,J.W., Johnston,S., Ahmed,R., Xie,V.K., Hubka,K.M., Cruz,L.,
            Nitschke,L., Stetsiv,M., Goering,J.P., Nistor,P., Lowell,S.,
            Hoskens,H., Claes,P., Weinberg,S.M., Saadi,I., Farach-Carson,M.C.
            and Fakhouri,W.D.
  TITLE     TWIST1 interacts with beta/delta-catenins during neural tube
            development and regulates fate transition in cranial neural crest
            cells
  JOURNAL   Development 149 (15) (2022)
   PUBMED   35781329
REFERENCE   4  (residues 1 to 1266)
  AUTHORS   Paul,B.J., Palmer,K.J., Rhea,L., Carlson,M., Sharp,J.C.,
            Pratt,C.H., Murray,S.A. and Dunnwald,M.
  TITLE     The Mafb cleft-associated variant H131Q is not required for
            palatogenesis in the mouse
  JOURNAL   Dev Dyn 250 (10), 1463-1476 (2021)
   PUBMED   33715275
REFERENCE   5  (residues 1 to 1266)
  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   6  (residues 1 to 1266)
  AUTHORS   Chintala,H., Krupska,I., Yan,L., Lau,L., Grant,M. and Chaqour,B.
  TITLE     The matricellular protein CCN1 controls retinal angiogenesis by
            targeting VEGF, Src homology 2 domain phosphatase-1 and Notch
            signaling
  JOURNAL   Development 142 (13), 2364-2374 (2015)
   PUBMED   26002917
REFERENCE   7  (residues 1 to 1266)
  AUTHORS   Ahmed,S.M., Theriault,B.L., Uppalapati,M., Chiu,C.W., Gallie,B.L.,
            Sidhu,S.S. and Angers,S.
  TITLE     KIF14 negatively regulates Rap1a-Radil signaling during breast
            cancer progression
  JOURNAL   J Cell Biol 199 (6), 951-967 (2012)
   PUBMED   23209302
REFERENCE   8  (residues 1 to 1266)
  AUTHORS   Leslie,E.J., Mansilla,M.A., Biggs,L.C., Schuette,K., Bullard,S.,
            Cooper,M., Dunnwald,M., Lidral,A.C., Marazita,M.L., Beaty,T.H. and
            Murray,J.C.
  TITLE     Expression and mutation analyses implicate ARHGAP29 as the
            etiologic gene for the cleft lip with or without cleft palate locus
            identified by genome-wide association on chromosome 1p22
  JOURNAL   Birth Defects Res A Clin Mol Teratol 94 (11), 934-942 (2012)
   PUBMED   23008150
REFERENCE   9  (residues 1 to 1266)
  AUTHORS   Xu,K., Sacharidou,A., Fu,S., Chong,D.C., Skaug,B., Chen,Z.J.,
            Davis,G.E. and Cleaver,O.
  TITLE     Blood vessel tubulogenesis requires Rasip1 regulation of GTPase
            signaling
  JOURNAL   Dev Cell 20 (4), 526-539 (2011)
   PUBMED   21396893
REFERENCE   10 (residues 1 to 1266)
  AUTHORS   Myagmar,B.E., Umikawa,M., Asato,T., Taira,K., Oshiro,M., Hino,A.,
            Takei,K., Uezato,H. and Kariya,K.
  TITLE     PARG1, a protein-tyrosine phosphatase-associated RhoGAP, as a
            putative Rap2 effector
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1046-1052 (2005)
   PUBMED   15752761
  REMARK    GeneRIF: These results suggest that PARG1 is a putative specific
            effector of Rap2 to regulate Rho.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100183.11.
            
            On Oct 7, 2017 this sequence version replaced XP_006501351.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            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 :: SRR10223969.4139.1,
                                           SRR10223970.5809.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1266
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="3"
                     /map="3 52.94 cM"
     Protein         1..1266
                     /product="rho GTPase-activating protein 29"
                     /note="PTPL1-associated RhoGAP 1; rho-type
                     GTPase-activating protein 29"
                     /calculated_mol_wt=142210
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355; propagated from
                     UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Region          220..436
                     /region_name="BAR"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain, a
                     dimerization module that binds membranes and detects
                     membrane curvature; cl12013"
                     /db_xref="CDD:472257"
     Region          482..501
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q52LW3; propagated from
                     UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Region          542..601
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5PQJ5; propagated from
                     UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Region          613..663
                     /region_name="C1_GMIP-like"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in the GEM-interacting protein (GMIP)-like family;
                     cd20816"
                     /db_xref="CDD:410366"
     Region          671..883
                     /region_name="RhoGAP"
                     /note="GTPase-activator protein (GAP) for Rho-like
                     GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases.
                     Small GTPases (G proteins) cluster into distinct families,
                     and all act as molecular switches, active in their
                     GTP-bound form but inactive when bound to...; cl02570"
                     /db_xref="CDD:470621"
     Site            order(709,746,750,843,846..847,874)
                     /site_type="other"
                     /note="GTPase interaction site"
                     /db_xref="CDD:239874"
     Site            709
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239874"
     Site            920
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5PQJ5; propagated from
                     UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Site            956
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q52LW3; propagated from
                     UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Site            1028
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q52LW3; propagated from
                     UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Region          1039..1081
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Region          1116..1157
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Site            1149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Site            1151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q52LW3; propagated from
                     UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Region          1209..1266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGF1.1)"
     Region          1263..1266
                     /region_name="Interaction with PTPN13/PTPL1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGF1.1)"
     CDS             1..1266
                     /gene="Arhgap29"
                     /gene_synonym="6720461J18Rik; A830014I19; B130017I01Rik;
                     Parg1"
                     /coded_by="NM_001356524.1:185..3985"
                     /db_xref="CCDS:CCDS17807.1"
                     /db_xref="GeneID:214137"
                     /db_xref="MGI:MGI:2443818"
ORIGIN      
        1 miahkqkkak kkrvwasgqp saaittsemg lksvsssssf dpeyikelvn dvrkfshmll
       61 ylkeailsdc fkevihirld ellrvlksil skhqnlssvd lqsaaevlta kvkavnftev
      121 neenkndifr evfssietla ftfgniltnf lmgdvgsdsi lrlpisresk sfenisvdsv
      181 dlphekgnfs pieldnlllk ntdsielals yaktwskytk nivswvekkl nlelestrni
      241 vklaeatrss igiqefmplq slftnallsd ihsshllqqt iaalqankfv qpllgrknem
      301 ekqrkeikdl wkqqqnklle tetalkkakl lcmqrqdeye kakssmfrae eeqlsssvgl
      361 aknlnkqlek rrrleeealq kveeanehyk vcvtnveerr ndlentkrei ltqlrtlvfq
      421 cdltlkavtv nlfhmqqlqa aslanslqsl cdsaklydpg qeysefvkat ssseleekvd
      481 gnvnkqmtns pqtsgyepad sledvarlpd schkleedrc snsadmtgps fvrswkfgmf
      541 sdsestggss esrsldsesi spgdfhrklp rtpssgtmss addlderepp spseagpnsl
      601 gafkktlmsk aalthkfrkl rsptkcrdcd givmfpgvec eecllvchrk clenlviicg
      661 hqklqgkmhi fgaefiqvak kepdgipfvl kicaseienr alclqgiyrv cgnkiktekl
      721 cqalengmhl vdisefsshd icdvlklylr qlpepfilfr lykefidlak eiqhvneeqe
      781 akkdspedkk hphvsievnr illkskdllr qlpashfnsl hyliahlrrv vdhaeenkmn
      841 sknlgvifgp tlirprptta pvtisslaey snqarlvefl itysqkifdg slqpqavvis
      901 ntgavapqvd qgylpkplls pderdtdhsm kplffssked irssdcesks felttsfees
      961 errqnalgkc daplldnkvh llfdqehesa sqkmedvcks pkllllksnr aansvqrhtp
     1021 rtkmrpvslp vdrllllass pterssrdvg nvdsdkfgkn pafeglhrkd nsnttrskvn
     1081 gfdqqnvqks wdtqyvrnnf takttmivps aypekgltvn tgnnrdhpgs kahaeparaa
     1141 gdvserrssd scpatavrap rtlqpqhwtt fykppnptfs vrgteektal psiavppvlv
     1201 hapqihvtks dpdseatlac pvqtsgqpke sseepalpeg tptcqrprlk rmqqfedled
     1261 eipqfv
//
