HMHA1_PONAB
ID HMHA1_PONAB Reviewed; 1163 AA.
AC Q5RB40;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=16774541; DOI=10.1111/j.1399-0039.2006.00603.x;
RA Wieles B., Pool J., Wilke M., Weber M., Kolb H.-J., Bontrop R.E.,
RA Goulmy E.;
RT "The diallelic locus encoding the minor histocompatibility antigen HA-1 is
RT evolutionarily conserved.";
RL Tissue Antigens 68:62-65(2006).
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; CR858815; CAH91020.1; -; mRNA.
DR RefSeq; NP_001127364.1; NM_001133892.1.
DR AlphaFoldDB; Q5RB40; -.
DR SMR; Q5RB40; -.
DR STRING; 9601.ENSPPYP00000010441; -.
DR GeneID; 100174429; -.
DR KEGG; pon:100174429; -.
DR CTD; 23526; -.
DR eggNOG; KOG1453; Eukaryota.
DR InParanoid; Q5RB40; -.
DR OrthoDB; 1300981at2759; -.
DR Proteomes; UP000001595; Unplaced.
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:0051056; P:regulation of small GTPase mediated signal transduction; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 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 Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF57889; SSF57889; 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; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..1163
FT /note="Rho GTPase-activating protein 45"
FT /id="PRO_0000330315"
FT DOMAIN 296..566
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 788..1001
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 729..774
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 118..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 403..526
FT /evidence="ECO:0000255"
FT COMPBIAS 16..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92619"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92619"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92619"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92619"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92619"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92619"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92619"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92619"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92619"
FT MOD_RES 976
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92619"
FT MOD_RES 1054
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TBD2"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TBD2"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TBD2"
SQ SEQUENCE 1163 AA; 127703 MW; 3D9CA2E2B058DF71 CRC64;
MFSRKKRELM KTPSISKKNR AGSPSPQPSG PHFISGETEA VSRPENPFNE LPSDLPKELP
RKDGADAVFP GTSLELPAGS SGVKATGTLK RPTSLSRHAS AAGFPLSGAA SWTLGRSHRS
PLTAASPGEL PTEGTGPDVV EDISHLLADV ARFAEGLEKL KECVLRDDLL EARRPLAHEC
LGEALRVMRQ IISKYPLLNT VETLTAAGTL IAKVKAFHYE SNNDLEKQEF EKALETIAVA
FSSAVSEFLM GEVDSSTLLA VPPGDSSQSM ESLYGSGSEG TPPSLDDCDA GCLPAEEVDV
LLQRCEGGVD AALLYAKNMA KYMKDLISYL EKRTTLEMEF AKGLQKMAHN CRQSVTQEPH
MPLLSIYSLA LEQDLEFGHG MVQAVGTLQT QTFMQPLTLR RLEHEKRRKE IKEAWHRAQR
KLQEAESNLR KAKQGYTQRC EDHDKARFLV AKAEEEQAGT APGAGSTATK TLDKRRRLEE
EAKNKAEEAM ATYRTCVADA KTQKQELEDT KVTALRQIQE VIRQSDQTIK SATISYYQMM
HMQTAPLPVH FQMLCESSKL YDPGQQYASH VRQLQRDQEP DVHYDFEPHV SANAWSPVMR
ARKSSFNVSD VAGPEAAGSP PEEGGCIEGT PVKGHRAGRG HQVHKSWPLS ISDSASGLDP
GPGAGDFKKF ERTSSSGTMS STEELVDPEG GAGASAFEQA DLNGMTPELP VAVPSGPFRH
EGLSKAARTH RLRKLRTPAK CRECNSYVYF QGAECEECCL ACHKKCLETL AIQCGHKKLQ
GRLQLFGQDF SHAARSAPDG VPFIVKKCVC EIERRALRTK GIYRVNGVKT RVEKLCQAFE
NGKELVELSQ ASPHDISNVL KLYLRQLPEP LISFRLYHEL VGLAKDSLKA EAEAKAASRG
RQDSSESEAV AVAMAGRLRE LLRDLPPENR ASLQYLLRHL RRIVEVEQDN KMTPGNLGIV
FGPTLLRPRP TEATVSLSSL VDYPHQARVI ETLIVHYGLV FEEEPEEIPG GQDESSNQRA
EVVVQVPYLE AGEGVVYPLQ EAAEDGCRES RVVSNDSDSD LEEASELLSS SEASALCRLS
FLEQQQSEAS LEEASGSHSG SEEQLETTAR EDGDGDEDSP AQRLSGFNTN QSNNVLQTPL
PPMRLRGGRI TLGSCRERQP EFV
