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Ras GTPase-activating protein 4 (Calcium-promoted Ras inactivator) (Ras p21 protein activator 4) (RasGAP-activating-like protein 2)

 RASL2_HUMAN             Reviewed;         803 AA.
O43374; O60286; Q14CQ4; Q86UW3; Q96QU0;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
15-AUG-2003, sequence version 2.
12-SEP-2018, entry version 162.
RecName: Full=Ras GTPase-activating protein 4;
AltName: Full=Calcium-promoted Ras inactivator;
AltName: Full=Ras p21 protein activator 4;
AltName: Full=RasGAP-activating-like protein 2;
Name=RASA4; Synonyms=CAPRI, GAPL, KIAA0538;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-352, FUNCTION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Blood;
PubMed=11448776; DOI=10.1016/S0960-9822(01)00261-5;
Lockyer P.J., Kupzig S., Cullen P.J.;
"CAPRI regulates Ca(2+)-dependent inactivation of the Ras-MAPK
pathway.";
Curr. Biol. 11:981-986(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:31-39(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
VAL-352.
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Ca(2+)-dependent Ras GTPase-activating protein, that
switches off the Ras-MAPK pathway following a stimulus that
elevates intracellular calcium. Functions as an adaptor for Cdc42
and Rac1 during FcR-mediated phagocytosis.
{ECO:0000269|PubMed:11448776}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:11448776}. Cell membrane
{ECO:0000269|PubMed:11448776}; Peripheral membrane protein
{ECO:0000269|PubMed:11448776}. Note=Localized to the cytosol as a
result of its lack of phosphoinositide binding activity. Upon
agonist-stimulated calcium mobilization, utilizes the C2A and C2B
domains to associate with the plasma membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O43374-1; Sequence=Displayed;
Name=2;
IsoId=O43374-2; Sequence=VSP_039965;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:11448776}.
-!- DOMAIN: The PH domain does not bind phosphatidylinositol 4,5-
bisphosphate or phosphatidylinositol 3,4,5-trisphosphate. This
lack of binding activity is due to Leu-592, compared to Arg found
in other family members.
-!- SEQUENCE CAUTION:
Sequence=AAB97935.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAP22345.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAA25464.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY029206; AAK31582.1; -; mRNA.
EMBL; AB011110; BAA25464.2; ALT_INIT; mRNA.
EMBL; AK026441; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC004084; AAB97935.2; ALT_SEQ; Genomic_DNA.
EMBL; AC093668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC105052; AAP22345.1; ALT_SEQ; Genomic_DNA.
EMBL; BC113663; AAI13664.1; -; mRNA.
CCDS; CCDS47674.1; -. [O43374-2]
CCDS; CCDS5725.1; -. [O43374-1]
RefSeq; NP_001073346.2; NM_001079877.2. [O43374-2]
RefSeq; NP_008920.5; NM_006989.5. [O43374-1]
UniGene; Hs.530089; -.
UniGene; Hs.656696; -.
ProteinModelPortal; O43374; -.
SMR; O43374; -.
BioGrid; 115458; 2.
IntAct; O43374; 4.
STRING; 9606.ENSP00000262940; -.
iPTMnet; O43374; -.
PhosphoSitePlus; O43374; -.
BioMuta; RASA4; -.
EPD; O43374; -.
MaxQB; O43374; -.
PaxDb; O43374; -.
PeptideAtlas; O43374; -.
PRIDE; O43374; -.
ProteomicsDB; 48913; -.
ProteomicsDB; 48914; -. [O43374-2]
DNASU; 10156; -.
Ensembl; ENST00000262940; ENSP00000262940; ENSG00000105808. [O43374-1]
Ensembl; ENST00000449970; ENSP00000412876; ENSG00000105808. [O43374-2]
GeneID; 10156; -.
KEGG; hsa:10156; -.
UCSC; uc003vae.4; human. [O43374-1]
CTD; 10156; -.
DisGeNET; 10156; -.
EuPathDB; HostDB:ENSG00000105808.17; -.
GeneCards; RASA4; -.
H-InvDB; HIX0034020; -.
H-InvDB; HIX0201129; -.
HGNC; HGNC:23181; RASA4.
HPA; HPA043010; -.
MIM; 607943; gene.
neXtProt; NX_O43374; -.
OpenTargets; ENSG00000105808; -.
PharmGKB; PA134889495; -.
eggNOG; KOG2059; Eukaryota.
eggNOG; ENOG410Y128; LUCA.
GeneTree; ENSGT00760000119092; -.
HOGENOM; HOG000234324; -.
HOVERGEN; HBG106587; -.
InParanoid; O43374; -.
KO; K17630; -.
OMA; DLGCDKT; -.
OrthoDB; EOG091G04T8; -.
PhylomeDB; O43374; -.
TreeFam; TF105302; -.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
ChiTaRS; RASA4; human.
GeneWiki; RASA4; -.
GenomeRNAi; 10156; -.
PRO; PR:O43374; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000105808; Expressed in 178 organ(s), highest expression level in muscle of leg.
CleanEx; HS_RASA4; -.
ExpressionAtlas; O43374; baseline and differential.
Genevisible; O43374; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IBA:GO_Central.
GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
GO; GO:0071277; P:cellular response to calcium ion; IMP:UniProtKB.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0034260; P:negative regulation of GTPase activity; IDA:CACAO.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IBA:GO_Central.
CDD; cd13372; PH_CAPRI; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 2.60.40.150; -; 2.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR039360; Ras_GTPase.
InterPro; IPR037777; RASA4_PH.
InterPro; IPR023152; RasGAP_CS.
InterPro; IPR001936; RasGAP_dom.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR001562; Znf_Btk_motif.
PANTHER; PTHR10194; PTHR10194; 1.
Pfam; PF00779; BTK; 1.
Pfam; PF00168; C2; 2.
Pfam; PF00169; PH; 1.
Pfam; PF00616; RasGAP; 1.
PRINTS; PR00360; C2DOMAIN.
SMART; SM00107; BTK; 1.
SMART; SM00239; C2; 2.
SMART; SM00233; PH; 1.
SMART; SM00323; RasGAP; 1.
SUPFAM; SSF48350; SSF48350; 1.
PROSITE; PS50004; C2; 2.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PROSITE; PS51113; ZF_BTK; 1.
2: Evidence at transcript level;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
GTPase activation; Membrane; Metal-binding; Polymorphism;
Reference proteome; Repeat; Zinc; Zinc-finger.
CHAIN 1 803 Ras GTPase-activating protein 4.
/FTId=PRO_0000056647.
DOMAIN 1 88 C2 1. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 129 216 C2 2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 302 512 Ras-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00167}.
DOMAIN 566 673 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
ZN_FING 675 711 Btk-type. {ECO:0000255|PROSITE-
ProRule:PRU00432}.
COMPBIAS 500 503 Poly-Leu.
VAR_SEQ 611 656 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_039965.
VARIANT 352 352 M -> V (in dbSNP:rs144395384).
{ECO:0000269|PubMed:11448776,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_027680.
VARIANT 432 432 R -> P (in dbSNP:rs886346).
/FTId=VAR_027681.
CONFLICT 213 213 G -> V (in Ref. 3; AK026441).
{ECO:0000305}.
CONFLICT 260 260 D -> G (in Ref. 3; AK026441).
{ECO:0000305}.
CONFLICT 429 429 R -> L (in Ref. 3; AK026441).
{ECO:0000305}.
CONFLICT 480 480 M -> V (in Ref. 3; AK026441).
{ECO:0000305}.
CONFLICT 606 606 T -> M (in Ref. 2; BAA25464).
{ECO:0000305}.
CONFLICT 752 752 A -> T (in Ref. 2; BAA25464).
{ECO:0000305}.
SEQUENCE 803 AA; 90458 MW; 6E70DBF2F8F5D0E9 CRC64;
MAKRSSLYIR IVEGKNLPAK DITGSSDPYC IVKVDNEPII RTATVWKTLC PFWGEEYQVH
LPPTFHAVAF YVMDEDALSR DDVIGKVCLT RDTIASHPKG FSGWAHLTEV DPDEEVQGEI
HLRLEVWPGA RACRLRCSVL EARDLAPKDR NGTSDPFVRV RYKGRTRETS IVKKSCYPRW
NETFEFELQE GAMEALCVEA WDWDLVSRND FLGKVVIDVQ RLRVVQQEEG WFRLQPDQSK
SRRHDEGNLG SLQLEVRLRD ETVLPSSYYQ PLVHLLCHEV KLGMQGPGQL IPLIEETTST
ECRQDVATNL LKLFLGQGLA KDFLDLLFQL ELSRTSETNT LFRSNSLASK SMESFLKVAG
MQYLHGVLGP IINKVFEEKK YVELDPSKVE VKDVGCSGLH RPQTEAEVLE QSAQTLRAHL
GALLSALSRS VRACPAVVRA TFRQLFRRVR ERFPGAQHEN VPFIAVTSFL CLRFFSPAIM
SPKLFHLRER HADARTSRTL LLLAKAVQNV GNMDTPASRA KEAWMEPLQP TVRQGVAQLK
DFITKLVDIE EKDELDLQRT LSLQAPPVKE GPLFIHRTKG KGPLMSSSFK KLYFSLTTEA
LSFAKTPSSK KSALIKLANI RAAEKVEEKS FGGSHVMQVI YTDDAGRPQT AYLQCKCVNE
LNQWLSALRK VSINNTGLLG SYHPGVFRGD KWSCCHQKEK TGQGCDKTRS RVTLQEWNDP
LDHDLEAQLI YRHLLGVEAM LWERHRELSG GAEAGTVPTS PGKVPEDSLA RLLRVLQDLR
EAHSSSPAGS PPSEPNCLLE LQT


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