SIPA1_MOUSE
ID SIPA1_MOUSE Reviewed; 1037 AA.
AC P46062; P70204;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Signal-induced proliferation-associated protein 1;
DE Short=Sipa-1;
DE AltName: Full=GTPase-activating protein Spa-1;
GN Name=Sipa1; Synonyms=Spa-1, Spa1;
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ;
RX PubMed=7799964; DOI=10.1128/mcb.15.1.552;
RA Hattori M., Tsukamoto N., Nur-E-Kamal M.S.A., Rubinfeld B., Iwai K.,
RA Kubota H., Maruta H., Minato N.;
RT "Molecular cloning of a novel mitogen-inducible nuclear protein with a Ran
RT GTPase-activating domain that affects cell cycle progression.";
RL Mol. Cell. Biol. 15:552-560(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 324-1037.
RC STRAIN=DBA/2J;
RX PubMed=9027487; DOI=10.1006/geno.1996.4464;
RA Wada Y., Kubota H., Maeda M., Taniwaki M., Hattori M., Imamura S., Iwai K.,
RA Minato N.;
RT "Mitogen-inducible SIPA1 is mapped to the conserved syntenic groups of
RT chromosome 19 in mouse and chromosome 11q13.3 centromeric to BCL1 in
RT human.";
RL Genomics 39:66-73(1997).
RN [3]
RP IDENTIFICATION OF PROBABLE FRAMESHIFTS.
RX PubMed=9346962; DOI=10.1074/jbc.272.44.28081;
RA Kurachi H., Wada Y., Tsukamoto N., Maeda M., Kubota H., Hattori M.,
RA Iwai K., Minato N.;
RT "Human SPA-1 product selectively expressed in lymphoid tissues is a
RT specific GTPase-activating protein for Rap1 and Rap2.";
RL J. Biol. Chem. 272:28081-28088(1997).
RN [4]
RP INTERACTION WITH RRP1B.
RX PubMed=18081427; DOI=10.1371/journal.pgen.0030214;
RA Crawford N.P., Qian X., Ziogas A., Papageorge A.G., Boersma B.J.,
RA Walker R.C., Lukes L., Rowe W.L., Zhang J., Ambs S., Lowy D.R.,
RA Anton-Culver H., Hunter K.W.;
RT "Rrp1b, a new candidate susceptibility gene for breast cancer progression
RT and metastasis.";
RL PLoS Genet. 3:E214-E214(2007).
RN [5]
RP 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-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Lung, Spleen, and Testis;
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: GTPase activator for the nuclear Ras-related regulatory
CC proteins Rap1, Rsr1 and Ran in vitro, converting them to the putatively
CC inactive GDP-bound state. Affects cell cycle progression.
CC {ECO:0000269|PubMed:7799964}.
CC -!- SUBUNIT: Interacts with RRP1B; the interaction leads to inhibition of
CC SIPA1 GTPase activity. {ECO:0000269|PubMed:18081427}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7799964}. Cytoplasm,
CC perinuclear region {ECO:0000250|UniProtKB:Q96FS4}. Endomembrane system;
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q96FS4}. Note=Mostly
CC localized in the perinuclear membraneous region.
CC {ECO:0000250|UniProtKB:Q96FS4}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in both fetal and adult
CC lymphohematopoietic tissues.
CC -!- INDUCTION: By mitogens.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA01973.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA13469.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D11374; BAA01973.1; ALT_FRAME; mRNA.
DR EMBL; D87849; BAA13469.1; ALT_INIT; Genomic_DNA.
DR PIR; I49709; I49709.
DR AlphaFoldDB; P46062; -.
DR SMR; P46062; -.
DR IntAct; P46062; 2.
DR STRING; 10090.ENSMUSP00000073618; -.
DR iPTMnet; P46062; -.
DR PhosphoSitePlus; P46062; -.
DR EPD; P46062; -.
DR jPOST; P46062; -.
DR MaxQB; P46062; -.
DR PaxDb; P46062; -.
DR PeptideAtlas; P46062; -.
DR PRIDE; P46062; -.
DR ProteomicsDB; 257180; -.
DR MGI; MGI:107576; Sipa1.
DR eggNOG; KOG3686; Eukaryota.
DR InParanoid; P46062; -.
DR PhylomeDB; P46062; -.
DR Reactome; R-MMU-392517; Rap1 signalling.
DR ChiTaRS; Sipa1; mouse.
DR PRO; PR:P46062; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P46062; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0042631; P:cellular response to water deprivation; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.11210; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF02145; Rap_GAP; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF111347; SSF111347; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; GTPase activation; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1037
FT /note="Signal-induced proliferation-associated protein 1"
FT /id="PRO_0000056745"
FT DOMAIN 316..534
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT DOMAIN 682..758
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 968..1025
FT /evidence="ECO:0000255"
FT COMPBIAS 855..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..969
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96FS4"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FS4"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FS4"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FS4"
FT MOD_RES 812
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FS4"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FS4"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FS4"
FT CONFLICT 738
FT /note="T -> A (in Ref. 2; BAA13469)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="R -> Q (in Ref. 2; BAA13469)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="T -> S (in Ref. 2; BAA13469)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1037 AA; 112066 MW; 2A30592E920A9AA5 CRC64;
MWAGGVGSPR RGMAPAPTDD LFARKLRQPA RPPLTPNTFE PRPARGPLLR SGSDAGEVRP
PTPASPRARA HSHEDASRPA ATPTRLFTDP LALLGLPAEE PEPTFPPVLE PRWFAHYDVQ
SLLFDWAPRP RGTGSHTEAN SGTLAEGQTT TSDLLLGAPG FVSELGGEGE LGLGGPISPP
VPPALPNAAV SVLEEPQTRT TTYSLEHADL GAGYYRKYFY GKEHQNFFGL DEALGPVAVS
LRREEKEGSG GGTLHSYRVI VRTTQLRTLR GTISEDALPP GPPSVSPRKL LEHVAPRLSP
TCLRLGSASP KVPRQLLTLD EQVLSFQRKG GILYCRAGQG SEEEMYNNQE AGAAFMQFLT
LLGDVVRLKG FESYRAQLDT KTDSTGTHSL YTTYQDHEIM FHVSTMLPYT PNNQQQLLRK
RHIGNDIVTI VFQEPGSKPF CPTTIRSHFQ HVFLVVRAHA PCTPHTSYRV AVSRTQDTPA
FGPALPEGGG PFAANADFRA FLLAKALNGE QAAGHARQFH AMATRTRQQY LQDLATNEVT
TTSLDSASRF GLPSLGGRRR ATPRSPGADV QAAGALMWGV RAAPGARVAA GAETSGPDDA
EVPCLLGISA ETLVLVAPRD GRVVFNCACR DVLAWTFSEH QLDLYHGRGE AITLRLDGAP
GQAVGEVVAR LQLVSRGCET RELALPRDGQ GRLGFEVDAE GFITHVERFT FAETTGLRPG
ARLLRVCGQT LPKLGPETAA QMLRSAPKVC VTVLPPDESG RPRRSFSELY MLSLKEPSRR
GGPEPVQDET GKLVILPPTK QLLHFCLKDS SSPPGPGDLT EERTEFLRTH NSLSSGSSLS
DEAPVLPNTT PDLLLVTTAN PSAPGTDRET PPSQDQSGSP SSHEDTSDSG PELRASILPR
TLSLRNSISK IMSEAGSETL EDEWQSISEI ASTCNTILES LSREGQPISE SGDPKEALKC
DSEPEPGSLS EKVSHLESML WKLQEDLQRE KADRAALEEE VRSLRHNNQR LLAESESAAT
RLLLASKHLG APTTDLA
