HMHA1_HUMAN
ID HMHA1_HUMAN Reviewed; 1136 AA.
AC Q92619; B4DTS4; F6QP70; Q6P189; Q7LE26; Q86WS1; Q8HX84; Q9GJN9; Q9GJP0;
AC Q9GJP1; Q9MY24;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Rho GTPase-activating protein 45 {ECO:0000312|HGNC:HGNC:17102};
DE Contains:
DE RecName: Full=Minor histocompatibility antigen HA-1;
DE Short=mHag HA-1;
GN Name=ARHGAP45 {ECO:0000312|HGNC:HGNC:17102};
GN Synonyms=HMHA1 {ECO:0000312|HGNC:HGNC:17102},
GN KIAA0223 {ECO:0000312|HGNC:HGNC:17102};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11095984; DOI=10.1006/bbrc.2000.3880;
RA Kaminski W.E., Piehler A., Schmitz G.;
RT "Genomic organization of the human cholesterol-responsive ABC transporter
RT ABCA7: tandem linkage with the minor histocompatibility antigen HA-1
RT gene.";
RL Biochem. Biophys. Res. Commun. 278:782-789(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS HIS-139;
RP ASP-259 AND GLY-439.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-140, AND VARIANT HIS-139.
RX PubMed=10958358; DOI=10.1034/j.1399-0039.2000.560109.x;
RA Arostegui J.I., Gallardo D., Rodriguez-Luaces M., Querol S., Madrigal J.A.,
RA Garcia-Lopez J., Granena A.;
RT "Genomic typing of minor histocompatibility antigen HA-1 by reference
RT strand mediated conformation analysis (RSCA).";
RL Tissue Antigens 56:69-76(2000).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-140, AND VARIANT HIS-139.
RX PubMed=16202172; DOI=10.1186/1471-2350-6-36;
RA Graziano C., Giorgi M., Malentacchi C., Mattiuz P.L., Porfirio B.;
RT "Sequence diversity within the HA-1 gene as detected by melting temperature
RT assay without oligonucleotide probes.";
RL BMC Med. Genet. 6:36-36(2005).
RN [9]
RP PROTEIN SEQUENCE OF 137-145, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP VARIANT HIS-139.
RX PubMed=9461441; DOI=10.1126/science.279.5353.1054;
RA den Haan J.M., Meadows L.M., Wang W., Pool J., Blokland E., Bishop T.L.,
RA Reinhardus C., Shabanowitz J., Offringa R., Hunt D.F., Engelhard V.H.,
RA Goulmy E.;
RT "The minor histocompatibility antigen HA-1: a diallelic gene with a single
RT amino acid polymorphism.";
RL Science 279:1054-1057(1998).
RN [10]
RP FUNCTION.
RX PubMed=8260714;
RA Marijt W.A.F., Veenhof W.F.J., Goulmy E., Willemze R., van Rood J.J.,
RA Falkenburg J.H.F.;
RT "Minor histocompatibility antigens HA-1-, -2-, and -4-, and HY-specific
RT cytotoxic T-cell clones inhibit human hematopoietic progenitor cell growth
RT by a mechanism that is dependent on direct cell-cell contact.";
RL Blood 82:3778-3785(1993).
RN [11]
RP FUNCTION.
RX PubMed=8532022; DOI=10.1056/nejm199602013340501;
RA Goulmy E., Schipper R., Pool J., Blokland E., Falkenburg J.H., Vossen J.,
RA Gratwohl A., Vogelsang G.B., van Houwelingen H.C., van Rood J.J.;
RT "Mismatches of minor histocompatibility antigens between HLA-identical
RT donors and recipients and the development of graft-versus-host disease
RT after bone marrow transplantation.";
RL N. Engl. J. Med. 334:281-285(1996).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=8843592; DOI=10.1016/s0966-3274(96)80009-8;
RA van Lochem E., van der Keur M., Mommaas A.M., de Gast G.C., Goulmy E.;
RT "Functional expression of minor histocompatibility antigens on human
RT peripheral blood dendritic cells and epidermal Langerhans cells.";
RL Transpl. Immunol. 4:151-157(1996).
RN [13]
RP FUNCTION.
RX PubMed=9798702; DOI=10.1097/00007890-199810150-00016;
RA Rufer N., Wolpert E., Helg C., Tiercy J.-M., Gratwohl A., Chapuis B.,
RA Jeannet M., Goulmy E., Roosnek E.;
RT "HA-1 and the SMCY-derived peptide FIDSYICQV (H-Y) are immunodominant minor
RT histocompatibility antigens after bone marrow transplantation.";
RL Transplantation 66:910-916(1998).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=11965046; DOI=10.1097/00007890-200204150-00022;
RA Fujii N., Hiraki A., Ikeda K., Ohmura Y., Nozaki I., Shinagawa K.,
RA Ishimaru F., Kiura K., Shimizu N., Tanimoto M., Harada M.;
RT "Expression of minor histocompatibility antigen, HA-1, in solid tumor
RT cells.";
RL Transplantation 73:1137-1141(2002).
RN [15]
RP FUNCTION.
RX PubMed=12601144; DOI=10.1073/pnas.0530192100;
RA Marijt W.A.E., Heemskerk M.H.M., Kloosterboer F.M., Goulmy E.,
RA Kester M.G.D., van der Hoorn M.A.W.G., van Luxemburg-Heys S.A.P.,
RA Hoogeboom M., Mutis T., Drijfhout J.W., van Rood J.J., Willemze R.,
RA Falkenburg J.H.F.;
RT "Hematopoiesis-restricted minor histocompatibility antigens HA-1- or HA-2-
RT specific T cells can induce complete remissions of relapsed leukemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2742-2747(2003).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-25, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-569, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-73; SER-93; SER-99;
RP SER-569 AND SER-619, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-73; SER-569 AND
RP SER-592, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=24086303; DOI=10.1371/journal.pone.0073962;
RA de Kreuk B.J., Schaefer A., Anthony E.C., Tol S., Fernandez-Borja M.,
RA Geerts D., Pool J., Hambach L., Goulmy E., Hordijk P.L.;
RT "The human minor histocompatibility antigen 1 is a RhoGAP.";
RL PLoS ONE 8:E73962-E73962(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-569; SER-578; SER-619
RP AND SER-949, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP VARIANT HIS-139.
RX PubMed=9820595; DOI=10.1111/j.1399-0039.1998.tb03052.x;
RA Tseng L.-H., Lin M.-T., Martin P.J., Pei J., Smith A.G., Hansen J.A.;
RT "Definition of the gene encoding the minor histocompatibility antigen HA-1
RT and typing for HA-1 from genomic DNA.";
RL Tissue Antigens 52:305-311(1998).
RN [25]
RP VARIANT HIS-139.
RX PubMed=16399573; DOI=10.1016/j.bbmt.2005.09.017;
RA Di Terlizzi S., Zino E., Mazzi B., Magnani C., Tresoldi C., Perna S.K.,
RA Bregni M., Rossini S., Ciceri F., Bordignon C., Bonini C., Fleischhauer K.;
RT "Therapeutic and diagnostic applications of minor histocompatibility
RT antigen HA-1 and HA-2 disparities in allogeneic hematopoietic stem cell
RT transplantation: a survey of different populations.";
RL Biol. Blood Marrow Transplant. 12:95-101(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:0000269|PubMed:24086303}.
CC -!- FUNCTION: Precursor of the histocompatibility antigen HA-1. More
CC generally, minor histocompatibility antigens (mHags) refer to
CC immunogenic peptide which, when complexed with MHC, can generate an
CC immune response after recognition by specific T-cells. The peptides are
CC derived from polymorphic intracellular proteins, which are cleaved by
CC normal pathways of antigen processing. The binding of these peptides to
CC MHC class I or class II molecules and its expression on the cell
CC surface can stimulate T-cell responses and thereby trigger graft
CC rejection or graft-versus-host disease (GVHD) after hematopoietic stem
CC cell transplantation from HLA-identical sibling donor. GVHD is a
CC frequent complication after bone marrow transplantation (BMT), due to
CC mismatch of minor histocompatibility antigen in HLA-matched sibling
CC marrow transplants. Specifically, mismatching for mHag HA-1 which is
CC recognized as immunodominant, is shown to be associated with the
CC development of severe GVHD after HLA-identical BMT. HA-1 is presented
CC to the cell surface by MHC class I HLA-A*0201, but also by other HLA-A
CC alleles. This complex specifically elicits donor-cytotoxic T-lymphocyte
CC (CTL) reactivity against hematologic malignancies after treatment by
CC HLA-identical allogenic BMT. It induces cell recognition and lysis by
CC CTL. {ECO:0000269|PubMed:12601144, ECO:0000269|PubMed:8260714,
CC ECO:0000269|PubMed:8532022, ECO:0000269|PubMed:9798702}.
CC -!- SUBUNIT: HA-1 forms a complex with MHC class I HLA-A*0201.
CC -!- INTERACTION:
CC Q92619; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-2825900, EBI-11975051;
CC Q92619; Q9P107: GMIP; NbExp=3; IntAct=EBI-2825900, EBI-11603420;
CC Q92619; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2825900, EBI-618309;
CC Q92619; O75031: HSF2BP; NbExp=3; IntAct=EBI-2825900, EBI-7116203;
CC Q92619; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-2825900, EBI-9640281;
CC Q92619; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-2825900, EBI-14066006;
CC Q92619; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-2825900, EBI-1105153;
CC Q92619; P63000: RAC1; NbExp=3; IntAct=EBI-2825900, EBI-413628;
CC Q92619; Q6NUQ1: RINT1; NbExp=5; IntAct=EBI-2825900, EBI-726876;
CC Q92619; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-2825900, EBI-11952721;
CC Q92619; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-2825900, EBI-9867283;
CC Q92619; Q96AP4: ZUP1; NbExp=3; IntAct=EBI-2825900, EBI-744706;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24086303}. Cell
CC projection, ruffle membrane {ECO:0000269|PubMed:24086303}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92619-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92619-2; Sequence=VSP_044707;
CC -!- TISSUE SPECIFICITY: Expressed on cells of the hematopoietic lineage.
CC Detected in dendritic cells and epidermal Langerhans cells. Expressed
CC in peripheral blood mononuclear cells, in all leukemia/lymphoma cell
CC lines. Detected also in some solid tumors and tissues such as cancerous
CC and non-cancerous tissue. {ECO:0000269|PubMed:11965046,
CC ECO:0000269|PubMed:8843592}.
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:0000269|PubMed:24086303}.
CC -!- POLYMORPHISM: The HA-1H allele is presented on the cell surface and
CC recognized by CTL, whereas the HA-1R allele is poorly represented by
CC HLA-A and non-immunogenic, although HA-1R allelic frequency is the
CC highest (PubMed:9820595, PubMed:16399573).
CC {ECO:0000269|PubMed:16399573, ECO:0000269|PubMed:9820595}.
CC -!- MISCELLANEOUS: Infusion of lymphocyte from mHag HA-1-negative donors
CC results in a durable remission in mHag HA-1-positive patients with
CC leukemia or multiple myeloma.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13212.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF308066; AAN04658.1; -; Genomic_DNA.
DR EMBL; AF308045; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308046; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308047; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308048; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308049; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308050; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308051; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308052; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308053; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308054; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308055; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308056; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308057; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308058; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308059; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308060; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308061; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308062; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308063; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308064; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF308065; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; AF311102; AAN04658.1; JOINED; Genomic_DNA.
DR EMBL; D86976; BAA13212.1; ALT_INIT; mRNA.
DR EMBL; AK300341; BAG62086.1; -; mRNA.
DR EMBL; AC004151; AAC03237.1; -; Genomic_DNA.
DR EMBL; AC011558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471139; EAW69551.1; -; Genomic_DNA.
DR EMBL; BC048129; AAH48129.1; -; mRNA.
DR EMBL; BC065223; AAH65223.1; -; mRNA.
DR EMBL; AF207595; AAG02014.1; -; Genomic_DNA.
DR EMBL; AF207596; AAG02015.1; -; Genomic_DNA.
DR EMBL; AF207597; AAG02016.1; -; Genomic_DNA.
DR EMBL; AF236756; AAF91292.1; -; Genomic_DNA.
DR CCDS; CCDS32863.1; -. [Q92619-1]
DR CCDS; CCDS58637.1; -. [Q92619-2]
DR PIR; D59433; D59433.
DR RefSeq; NP_001245257.1; NM_001258328.2. [Q92619-2]
DR RefSeq; NP_001269263.1; NM_001282334.1.
DR RefSeq; NP_001269264.1; NM_001282335.1.
DR RefSeq; NP_036424.2; NM_012292.4. [Q92619-1]
DR PDB; 3D25; X-ray; 1.30 A; C=140-145.
DR PDB; 3FT3; X-ray; 1.95 A; P=137-145.
DR PDBsum; 3D25; -.
DR PDBsum; 3FT3; -.
DR AlphaFoldDB; Q92619; -.
DR SMR; Q92619; -.
DR BioGRID; 117072; 19.
DR IntAct; Q92619; 20.
DR STRING; 9606.ENSP00000439601; -.
DR GlyGen; Q92619; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q92619; -.
DR PhosphoSitePlus; Q92619; -.
DR SwissPalm; Q92619; -.
DR BioMuta; ARHGAP45; -.
DR DMDM; 187471158; -.
DR EPD; Q92619; -.
DR jPOST; Q92619; -.
DR MassIVE; Q92619; -.
DR MaxQB; Q92619; -.
DR PaxDb; Q92619; -.
DR PeptideAtlas; Q92619; -.
DR PRIDE; Q92619; -.
DR ProteomicsDB; 27852; -.
DR ProteomicsDB; 75372; -. [Q92619-1]
DR Antibodypedia; 10356; 184 antibodies from 29 providers.
DR DNASU; 23526; -.
DR Ensembl; ENST00000313093.7; ENSP00000316772.2; ENSG00000180448.11. [Q92619-1]
DR Ensembl; ENST00000539243.6; ENSP00000439601.1; ENSG00000180448.11. [Q92619-2]
DR GeneID; 23526; -.
DR KEGG; hsa:23526; -.
DR MANE-Select; ENST00000313093.7; ENSP00000316772.2; NM_012292.5; NP_036424.2.
DR UCSC; uc002lqz.4; human. [Q92619-1]
DR CTD; 23526; -.
DR DisGeNET; 23526; -.
DR GeneCards; ARHGAP45; -.
DR HGNC; HGNC:17102; ARHGAP45.
DR HPA; ENSG00000180448; Group enriched (bone marrow, intestine, lung, lymphoid tissue).
DR MIM; 601155; gene.
DR neXtProt; NX_Q92619; -.
DR NIAGADS; ENSG00000180448; -.
DR OpenTargets; ENSG00000180448; -.
DR PharmGKB; PA128394633; -.
DR VEuPathDB; HostDB:ENSG00000180448; -.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT00950000183110; -.
DR HOGENOM; CLU_006236_0_1_1; -.
DR InParanoid; Q92619; -.
DR OMA; IMLQRCE; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; Q92619; -.
DR TreeFam; TF351450; -.
DR PathwayCommons; Q92619; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; Q92619; -.
DR BioGRID-ORCS; 23526; 39 hits in 1080 CRISPR screens.
DR ChiTaRS; ARHGAP45; human.
DR EvolutionaryTrace; Q92619; -.
DR GeneWiki; HMHA1; -.
DR GenomeRNAi; 23526; -.
DR Pharos; Q92619; Tbio.
DR PRO; PR:Q92619; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q92619; protein.
DR Bgee; ENSG00000180448; Expressed in granulocyte and 156 other tissues.
DR ExpressionAtlas; Q92619; baseline and differential.
DR Genevisible; Q92619; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
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:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
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 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasm; Direct protein sequencing; GTPase activation;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..1136
FT /note="Rho GTPase-activating protein 45"
FT /id="PRO_0000330312"
FT PEPTIDE 137..145
FT /note="Minor histocompatibility antigen HA-1"
FT /id="PRO_0000330313"
FT DOMAIN 269..539
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 761..974
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 702..747
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 376..412
FT /evidence="ECO:0000255"
FT COILED 440..499
FT /evidence="ECO:0000255"
FT COMPBIAS 1061..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19367720,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1027
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TBD2"
FT MOD_RES 1030
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TBD2"
FT MOD_RES 1032
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TBD2"
FT VAR_SEQ 1..30
FT /note="MFSRKKRELMKTPSISKKNRAGSPSPQPSG -> MSRGQRVLKGLLGWVCTW
FT TWAWRARLGARGCGLHVLCPRDLPLPPE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044707"
FT VARIANT 139
FT /note="R -> H (in allele HA-1H; induction of CTL
FT recognition for epitope HA-1; dbSNP:rs1801284)"
FT /evidence="ECO:0000269|PubMed:10958358,
FT ECO:0000269|PubMed:16202172, ECO:0000269|PubMed:16399573,
FT ECO:0000269|PubMed:9461441, ECO:0000269|PubMed:9820595,
FT ECO:0000269|Ref.5"
FT /id="VAR_042693"
FT VARIANT 259
FT /note="E -> D (in dbSNP:rs2074442)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_042694"
FT VARIANT 439
FT /note="S -> G (in dbSNP:rs7251797)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_042695"
FT VARIANT 515
FT /note="M -> I (in dbSNP:rs36084354)"
FT /id="VAR_042696"
FT VARIANT 886
FT /note="A -> P (in dbSNP:rs34569196)"
FT /id="VAR_042697"
FT CONFLICT 648
FT /note="S -> F (in Ref. 3; BAG62086)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1136 AA; 124614 MW; 9536787B3B1EE16D CRC64;
MFSRKKRELM KTPSISKKNR AGSPSPQPSG ELPRKDGADA VFPGPSLEPP AGSSGVKATG
TLKRPTSLSR HASAAGFPLS GAASWTLGRS HRSPLTAASP GELPTEGAGP DVVEDISHLL
ADVARFAEGL EKLKECVLRD DLLEARRPRA HECLGEALRV MHQIISKYPL LNTVETLTAA
GTLIAKVKAF HYESNNDLEK QEFEKALETI AVAFSSTVSE FLMGEVDSST LLAVPPGDSS
QSMESLYGPG SEGTPPSLED CDAGCLPAEE VDVLLQRCEG GVDAALLYAK NMAKYMKDLI
SYLEKRTTLE MEFAKGLQKI AHNCRQSVMQ EPHMPLLSIY SLALEQDLEF GHSMVQAVGT
LQTQTFMQPL TLRRLEHEKR RKEIKEAWHR AQRKLQEAES NLRKAKQGYV QRCEDHDKAR
FLVAKAEEEQ AGSAPGAGST ATKTLDKRRR LEEEAKNKAE EAMATYRTCV ADAKTQKQEL
EDTKVTALRQ IQEVIRQSDQ TIKSATISYY QMMHMQTAPL PVHFQMLCES SKLYDPGQQY
ASHVRQLQRD QEPDVHYDFE PHVSANAWSP VMRARKSSFN VSDVARPEAA GSPPEEGGCT
EGTPAKDHRA GRGHQVHKSW PLSISDSDSG LDPGPGAGDF KKFERTSSSG TMSSTEELVD
PDGGAGASAF EQADLNGMTP ELPVAVPSGP FRHEGLSKAA RTHRLRKLRT PAKCRECNSY
VYFQGAECEE CCLACHKKCL ETLAIQCGHK KLQGRLQLFG QDFSHAARSA PDGVPFIVKK
CVCEIERRAL RTKGIYRVNG VKTRVEKLCQ AFENGKELVE LSQASPHDIS NVLKLYLRQL
PEPLISFRLY HELVGLAKDS LKAEAEAKAA SRGRQDGSES EAVAVALAGR LRELLRDLPP
ENRASLQYLL RHLRRIVEVE QDNKMTPGNL GIVFGPTLLR PRPTEATVSL SSLVDYPHQA
RVIETLIVHY GLVFEEEPEE TPGGQDESSN QRAEVVVQVP YLEAGEAVVY PLQEAAADGC
RESRVVSNDS DSDLEEASEL LSSSEASALG HLSFLEQQQS EASLEVASGS HSGSEEQLEA
TAREDGDGDE DGPAQQLSGF NTNQSNNVLQ APLPPMRLRG GRMTLGSCRE RQPEFV
