ID HMHA1_XENLA Reviewed; 1107 AA.
AC Q6DE55;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Rho GTPase-activating protein 45 {ECO:0000250|UniProtKB:Q92619};
DE AltName: Full=Minor histocompatibility protein HA-1 {ECO:0000250|UniProtKB:Q92619};
GN Name=arhgap45 {ECO:0000250|UniProtKB:Q92619};
GN Synonyms=hmha1 {ECO:0000250|UniProtKB:Q92619};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Contains a GTPase activator for the Rho-type GTPases (RhoGAP)
CC domain that would be able to negatively regulate the actin cytoskeleton
CC as well as cell spreading. However, also contains N-terminally a BAR-
CC domin which is able to play an autoinhibitory effect on this RhoGAP
CC activity. {ECO:0000250|UniProtKB:Q92619}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92619}. Cell
CC projection, ruffle membrane {ECO:0000250|UniProtKB:Q92619}.
CC -!- DOMAIN: Rho-GAP domain is able to regulate RhoGTPase activity, actin
CC cytoskeleton and cell spreading. However N-terminally BAR domain plays
CC an autoinhibitory role. {ECO:0000250|UniProtKB:Q92619}.
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DR EMBL; BC077287; AAH77287.1; -; mRNA.
DR RefSeq; NP_001086672.1; NM_001093203.1.
DR AlphaFoldDB; Q6DE55; -.
DR SMR; Q6DE55; -.
DR GeneID; 446507; -.
DR KEGG; xla:446507; -.
DR AGR; Xenbase:XB-GENE-990083; -.
DR CTD; 446507; -.
DR Xenbase; XB-GENE-990083; arhgap45.L.
DR OrthoDB; 5395569at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 446507; Expressed in spleen and 18 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20816; C1_GMIP-like; 1.
DR CDD; cd04409; RhoGAP_PARG1; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR15228:SF18; RHO GTPASE-ACTIVATING PROTEIN 45; 1.
DR PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm; GTPase activation;
KW Membrane; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1107
FT /note="Rho GTPase-activating protein 45"
FT /id="PRO_0000330316"
FT DOMAIN 261..524
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 730..942
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 671..716
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 103..132
FT /evidence="ECO:0000255"
FT COILED 363..485
FT /evidence="ECO:0000255"
FT COMPBIAS 16..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1107 AA; 123527 MW; B6E5D890B0499F89 CRC64;
MFSRKKRELM KTPSLSKKSR AGSPAPQNDL TRKDVTDSSN DLASSPPSNS SPVSSGTLKR
PSSLSRHASA AGIPLSSPRG KATKPASTPS PPESGEGPFI DVEDISQLLG DVARFAERLE
KLRDVVQDEE LKETRRPLAH ECLGEALRLL RQVINKYPLL NTVETLTAAG TLISKVKGFH
YESSIENDKR DFEKALESMA VCFSSTISEF LMGEVDSSTL LSLPPGDQSQ SMESLCGGLS
GGEGALPSAH EYVEAGGHLG EDVDVILQRS DGGVQAALLY AKNMAKYLKD LSSYIEKRTI
LEMEYAKGLQ KLVNAYKGTL NQETHMPFQS IYSVALEQDL EHGHGILHTA LTLQHQTFLQ
PINMRRQEHE KRRKEVKEQW QRAQRKLMEA ESNLRKARQA YMQRSEEHER ALYNATRAEE
EQSHSGTRSL DKKRRAEEEA KNRAEEAMAT YRTCIADAKT QKQELEDVKV NVLRQLQELI
KQSDQILRSA TISYYQSMHM QTAPLPVGFQ MLCESSKLYD LGQQYASYVR QLGAVNEPET
SYDFQPYTPQ ITWSPCIRAR KSSFNSQDIP SSENKEISGE ERGVERRGGR GHQVHKSWPT
AITEGDPAVS SATVPAFPEK LHQPLSPTEN VDQKRLSASF EQSINGLSGS LEVQNSTGPF
RNIGLSRAAL THRLRKLRTP SKCRECNSYV YFQGAECEEC SLACHKKCLE TLAIQCGHKK
LQGRLLLFGR DFSETALRSP DHIPFLIRKC VSEIEERALI MKGIYRVNGV KTRVEKLCQA
FENGKELVEL SQASPHDLSN VLKLYLRQLP EPLIPFRLYN GLMGLAKESL RGTETGKGPR
LQDKGPNTET DVLSIVVQLK ELLQDLPSEN RTTLQYLVKH LCRVSEQEQL NKMSPSNLGI
VFGPALMRPR PTDATVSLSS LVDYPHQARI VETLIIFYST IFQEPVSNTD IGTGNSSSDD
TASMQSRARL QVTVEEDLSE LTPEYQIPVF KEPGASTVES DSESDGAEDI PGTWKPQTTR
GHLTKEASVT SAEDIPYIEG EAQSESEEDR DQTQENLAEN NTNQSNNVAV NGHCCVPHFH
CHTQLPAIRM MHGKIYVSSA DRRPHFV
//
