HMHA1_MOUSE
ID HMHA1_MOUSE Reviewed; 1116 AA.
AC Q3TBD2; Q3TDD2; Q3TSW0; Q3TXM6; Q3UZ72; Q8BI83; Q9CU46;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Rho GTPase-activating protein 45 {ECO:0000312|MGI:MGI:1917969};
DE AltName: Full=Minor histocompatibility protein HA-1;
GN Name=Arhgap45 {ECO:0000312|MGI:MGI:1917969};
GN Synonyms=Hmha1 {ECO:0000312|MGI:MGI:1917969};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Medulla oblongata, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-577; SER-1017;
RP SER-1020 AND SER-1022, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-577; SER-1017; SER-1020 AND
RP SER-1022, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-568; SER-577;
RP SER-591; SER-618; SER-1017; SER-1020 AND SER-1022, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q3TBD2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TBD2-2; Sequence=VSP_033031, VSP_033032;
CC Name=3;
CC IsoId=Q3TBD2-3; Sequence=VSP_033030;
CC Name=4;
CC IsoId=Q3TBD2-4; Sequence=VSP_033029;
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; AK018130; BAB31085.1; -; mRNA.
DR EMBL; AK044860; BAC32124.1; -; mRNA.
DR EMBL; AK134029; BAE21986.1; -; mRNA.
DR EMBL; AK159194; BAE34889.1; -; mRNA.
DR EMBL; AK161766; BAE36565.1; -; mRNA.
DR EMBL; AK170262; BAE41670.1; -; mRNA.
DR EMBL; AK171304; BAE42381.1; -; mRNA.
DR EMBL; BC053750; AAH53750.1; -; mRNA.
DR CCDS; CCDS24005.1; -. [Q3TBD2-2]
DR CCDS; CCDS48624.1; -. [Q3TBD2-1]
DR RefSeq; NP_001136173.1; NM_001142701.1.
DR RefSeq; NP_001334003.1; NM_001347074.1.
DR RefSeq; NP_081797.1; NM_027521.3. [Q3TBD2-2]
DR AlphaFoldDB; Q3TBD2; -.
DR SMR; Q3TBD2; -.
DR BioGRID; 214219; 2.
DR IntAct; Q3TBD2; 3.
DR STRING; 10090.ENSMUSP00000097100; -.
DR iPTMnet; Q3TBD2; -.
DR PhosphoSitePlus; Q3TBD2; -.
DR EPD; Q3TBD2; -.
DR jPOST; Q3TBD2; -.
DR MaxQB; Q3TBD2; -.
DR PaxDb; Q3TBD2; -.
DR PeptideAtlas; Q3TBD2; -.
DR PRIDE; Q3TBD2; -.
DR ProteomicsDB; 273117; -. [Q3TBD2-1]
DR ProteomicsDB; 273118; -. [Q3TBD2-2]
DR ProteomicsDB; 273119; -. [Q3TBD2-3]
DR ProteomicsDB; 273120; -. [Q3TBD2-4]
DR Antibodypedia; 10356; 184 antibodies from 29 providers.
DR DNASU; 70719; -.
DR Ensembl; ENSMUST00000043311; ENSMUSP00000041019; ENSMUSG00000035697. [Q3TBD2-2]
DR GeneID; 70719; -.
DR KEGG; mmu:70719; -.
DR UCSC; uc007gbe.2; mouse. [Q3TBD2-1]
DR UCSC; uc007gbg.2; mouse. [Q3TBD2-2]
DR CTD; 23526; -.
DR MGI; MGI:1917969; Arhgap45.
DR VEuPathDB; HostDB:ENSMUSG00000035697; -.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT00950000183110; -.
DR InParanoid; Q3TBD2; -.
DR PhylomeDB; Q3TBD2; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 70719; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Arhgap45; mouse.
DR PRO; PR:Q3TBD2; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q3TBD2; protein.
DR Bgee; ENSMUSG00000035697; Expressed in granulocyte and 110 other tissues.
DR ExpressionAtlas; Q3TBD2; baseline and differential.
DR Genevisible; Q3TBD2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasm; GTPase activation; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1116
FT /note="Rho GTPase-activating protein 45"
FT /id="PRO_0000330314"
FT DOMAIN 268..538
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 758..971
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 699..744
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 375..498
FT /evidence="ECO:0000255"
FT COMPBIAS 16..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92619"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92619"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92619"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 946
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92619"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1020
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1022
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..461
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033029"
FT VAR_SEQ 1..309
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033030"
FT VAR_SEQ 1..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_033031"
FT VAR_SEQ 117..139
FT /note="TLLADVARFAEGLEKLKECVLQD -> MCVCGTLHPALDHDPLCCQTRAR
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_033032"
FT CONFLICT 87
FT /note="V -> G (in Ref. 1; BAE34889/BAE41670)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="E -> K (in Ref. 1; BAE21986)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="K -> E (in Ref. 1; BAE34889)"
FT /evidence="ECO:0000305"
FT CONFLICT 979
FT /note="P -> H (in Ref. 1; BAB31085)"
FT /evidence="ECO:0000305"
FT CONFLICT 1047
FT /note="Q -> R (in Ref. 1; BAE41670/BAE42381)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1116 AA; 122902 MW; E3F52D0364F19E96 CRC64;
MFSRKKRELM KTPSISKKNR AGSPNPQSSS GELPRKDWTE APGLEPPATS LSTVAKGTGT
LKRPTSLSRH ASAAGFPLSG TATWTLVRGY RSPLSAASPA ELPTEGAFPD GVEDISTLLA
DVARFAEGLE KLKECVLQDD LLEARRPLAH ECLGEALRVM RQVISRYPLL NTVETLTAAG
TLIAKVKAFH YECNNESDKR EFEKALETIA VSFSCTVSEF LLGEVDSSTL LAVPPGDPSQ
SMENLYGAGT EGPPHNVEEC EEGCLPPEEV DMLLQRCEGG VDAALQYAKD MARYMKDLIS
YLEKRTTLEM EFAKGLQKVV HNCRQSVTHE PHMPLLSIYS LALEQDLEFG HGMVQAAGTL
QTQTFMQPLT LRRLEHERRR KEIKESWHRA QRKLQEAEAN LRKAKQGYKQ RCEDHDKARL
QVAKAEEEQQ GTGPGAGTAA SKALDKRRRL EEEAKNKAEE AMATYRTCVA DAKTQKQELE
DTKVTALRQI QEVIRQSDQT IKSATISYYQ LMHMQTAPLP VNFQMLCESS KLYDPGQQYA
SHVRQLQRGE EPDVRYDFEP YVSNNSWSPI MRTRKGSFNP GDASGPEAAG SPPEEGGTSE
AAPNKDHRGG RGHQVHKSWP ISISDTEVGL DTSSGDLKKF DRTSSSGTMS SSEELGDQEA
GLVASAFDSA DLNGMDPELP VAMPSGPFRH VGLSKAARTH RLRKLRTPAK CRECNSYVYF
QGAECEECCL ACHKKCLETL AIQCGHKKLQ GRLQLFGQDF SQAALSTPDG VPFIVKKCVC
EIERRALHTK GIYRVNGVKT RVEKLCQAFE NGKELVELSQ ASPHDISNVL KLYLRQLPEP
LISFRFYHEL VGLAKDSLKA EAEAKAASRG RQGGSESEAA TLAMVGRLRE LMQDLPAENR
ATLLYLLKHL RRIVEMEQDN KMTPGNLGIV FGPTLLRPRP TDATVSLSSL VDYPHQARVI
ETLIVHYGLV FEEEPEEAPG SQEGASTQCG QLESAEGIVF PLQEEAEDGS RESHAASNDS
DSELEDASDP LSSSDASALH RLSFLEQTEA GLEEGPQSHS GSEEQLEGED GAPGPWLCHF
NTNQSNNTSR APLPTMRLRG GQITGGTSQE RQPQFV
