SI1L3_MOUSE
ID SI1L3_MOUSE Reviewed; 1776 AA.
AC G3X9J0;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Signal-induced proliferation-associated 1-like protein 3;
DE Short=SIPA1-like protein 3;
DE AltName: Full=SPA-1-like protein 3;
GN Name=Sipa1l3; Synonyms=Spal3;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1538, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; SER-140; SER-1358;
RP THR-1381; SER-1538; SER-1541; SER-1614; SER-1617; SER-1672 AND THR-1698,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, 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).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=26231217; DOI=10.1093/hmg/ddv298;
RA Greenlees R., Mihelec M., Yousoof S., Speidel D., Wu S.K., Rinkwitz S.,
RA Prokudin I., Perveen R., Cheng A., Ma A., Nash B., Gillespie R.,
RA Loebel D.A., Clayton-Smith J., Lloyd I.C., Grigg J.R., Tam P.P., Yap A.S.,
RA Becker T.S., Black G.C., Semina E., Jamieson R.V.;
RT "Mutations in SIPA1L3 cause eye defects through disruption of cell polarity
RT and cytoskeleton organization.";
RL Hum. Mol. Genet. 24:5789-5804(2015).
CC -!- FUNCTION: Plays a critical role in epithelial cell morphogenesis,
CC polarity, adhesion and cytoskeletal organization in the lens
CC (PubMed:26231217). {ECO:0000269|PubMed:26231217}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:O60292}. Note=Detected in tricellular junctions.
CC Colocalizes with apical F-actin. {ECO:0000250|UniProtKB:O60292}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing lens.
CC {ECO:0000269|PubMed:26231217}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice at 4 weeks postnatal age show
CC reduced lens size and microphthalmia (PubMed:26231217).
CC {ECO:0000269|PubMed:26231217}.
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DR EMBL; AC164640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC166079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466593; EDL24066.1; -; Genomic_DNA.
DR CCDS; CCDS39871.1; -.
DR RefSeq; NP_001074497.1; NM_001081028.1.
DR RefSeq; XP_011249034.1; XM_011250732.2.
DR AlphaFoldDB; G3X9J0; -.
DR SMR; G3X9J0; -.
DR IntAct; G3X9J0; 1.
DR STRING; 10090.ENSMUSP00000082965; -.
DR iPTMnet; G3X9J0; -.
DR PhosphoSitePlus; G3X9J0; -.
DR EPD; G3X9J0; -.
DR jPOST; G3X9J0; -.
DR MaxQB; G3X9J0; -.
DR PaxDb; G3X9J0; -.
DR PeptideAtlas; G3X9J0; -.
DR PRIDE; G3X9J0; -.
DR ProteomicsDB; 261228; -.
DR Antibodypedia; 59222; 71 antibodies from 21 providers.
DR DNASU; 74206; -.
DR Ensembl; ENSMUST00000085809; ENSMUSP00000082965; ENSMUSG00000030583.
DR Ensembl; ENSMUST00000183096; ENSMUSP00000138171; ENSMUSG00000030583.
DR GeneID; 74206; -.
DR KEGG; mmu:74206; -.
DR UCSC; uc009gbs.1; mouse.
DR CTD; 23094; -.
DR MGI; MGI:1921456; Sipa1l3.
DR VEuPathDB; HostDB:ENSMUSG00000030583; -.
DR eggNOG; KOG3686; Eukaryota.
DR GeneTree; ENSGT00940000159183; -.
DR HOGENOM; CLU_002127_0_0_1; -.
DR InParanoid; G3X9J0; -.
DR OMA; WVQNGSM; -.
DR OrthoDB; 28453at2759; -.
DR PhylomeDB; G3X9J0; -.
DR TreeFam; TF318626; -.
DR BioGRID-ORCS; 74206; 4 hits in 72 CRISPR screens.
DR PRO; PR:G3X9J0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; G3X9J0; protein.
DR Bgee; ENSMUSG00000030583; Expressed in epithelium of small intestine and 218 other tissues.
DR ExpressionAtlas; G3X9J0; baseline and differential.
DR GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0061689; C:tricellular tight junction; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IMP:UniProtKB.
DR GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP: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 InterPro; IPR031204; SIPA1L3.
DR InterPro; IPR021818; SIPA1L_C.
DR PANTHER; PTHR15711:SF15; PTHR15711:SF15; 1.
DR Pfam; PF02145; Rap_GAP; 1.
DR Pfam; PF11881; SPAR_C; 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 Acetylation; Cell membrane; Coiled coil; GTPase activation; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1776
FT /note="Signal-induced proliferation-associated 1-like
FT protein 3"
FT /id="PRO_0000435476"
FT DOMAIN 605..822
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT DOMAIN 960..1024
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 41..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1715..1769
FT /evidence="ECO:0000255"
FT COMPBIAS 46..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1589..1603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60292"
FT MOD_RES 1358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1381
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1442
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60292"
FT MOD_RES 1538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1694
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60292"
FT MOD_RES 1698
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1776 AA; 195063 MW; AD19E1C84BA720CE CRC64;
MTTYRPLPND GVDLAASCGA RSTDILPGPH PGDYTPMGFW AQNGSMPQPL GESPAATTTR
PSPTTPAMPK MGVRARVADW PPKRDALREQ SNPSPSQDTD GVKTTKVAHS MRNLQNGQLP
SSTPASSGSR AFHRLSRRRS KDVEFQDGWP RSPGRAFLPL RHRSSSEITL SECDVEEPGD
PRGTRHPGVL PLFREYGSTS SIDVQGVPEQ SFFDILNEFR SEQPEARGSQ NLRELLQVDP
GALSGGSCGT KGDPRNGQPT KDSLQSLQPL KEKEKSRKKP VRGLGSGDTV DSSIFRKLRS
SKPEGEVGRP LGETEESRSP PEASRPWVCQ KSFAHFDVQS MLFDLNEAAA NRVSVAQRRN
TTTGASAASA ASAMVTLTAS RAHSLGTLDP AFTSTEDLNC KENLEQDLGD DNSNDLLLSC
PHFRNEIGGE RERNVSFSRA SVGSPGGSSE AHMAEPTLST HRTNASISVL EVPKEQQRTQ
SRPRQYSIEH VDLGARYYQD YFVGKEHANY FGVDEKLGPV AVSIKREKLE DHKDHGPQYQ
YRIIFRTREL ITLRGSILED ATPTATKHGT GRGLPLKDAL EYVIPELNIH CLRLALNTPK
VTEQLLKLDE QGLCRKHKVG ILYCKAGQSS EEEMYNNEEA GPAFEEFLDL LGDKVCLKGF
TKYAAQLDVK TDSTGTHSLY TTYQDYEIMF HVSTLLPYTP NNRQQLLRKR HIGNDIVTII
FQEPGALPFT PKNIRSHFQH VFIIVRVHNP CTENVCYSMA VTRSKDAPPF GPPIPNGTTF
RKSDVFRDFL LAKVINAENA AHKSDKFHTM ATRTRQEYLK DLAENCVSNT PIDSSGKFNL
ISLTSKKKEK TKARAGAEQH SAGAIAWRVA AQDYAQGSEI DCILGISNEF VVLLDLRTKE
VVFNCYCGDV IGWTPDSSTI KIFYGRGDHI FLQAAEGSVE DIRDIVQRLK VMTNGWETVD
MTLRRNGLGQ LGFHVKYDGT VAEVEDYGFA WQAGLRQGSR LVEICKVAVV TLSHDQMIDL
LRTSVTVKVV IIPPFEDGTP RRGWPETYDM NASEPKTESE TTTPGGRPPY RSNAPWQWSG
PASHNSLPAT KWTTPATPGH AQSLSRLPKQ TPVVPFRESQ PLHSKRPVSF PETPFAASPA
GADRVPPYRQ PSGSFSTPGS ATYARYKPSP ERYAAAPHPL LSFDPHFMHD GMSSGDSSSG
GLTSQESTME RPKPEPLWHV PAQARLSAMT GSIGSKHPSR QDAAGKDSPN RHSKGEPQYS
SHSSSNTLSS NASSSHSDDR WFDPLDPLEP EQDPFSKGGS SDSGIDTTLY TSSPSCMSLA
KAPRPTKPHK PPGNIGLCGG GRESAGRPHP VDRRREVSPA PVVAGQNKGY RPKLYSSGSC
TPPGLVGGSR DPPRQPSDMG SRAGYPTQVY KTASAETPRP SQLSQCSPFQ LSTSVPKSFF
SKQPAHNKHS TGWKRTDEPP PRPLPFTDSK KQVDTNAKNV FGQPRLRASL RDLRSPRKNY
KSTIEDDLKK LIVMDNLGPE QERDTGQSPQ KSLQRTLSDE SLCSGRREPS FASPASLEPG
LPSDVLFTST CTFPSSTLPA RRQHQHAHPP SGAPSTTPAT GNGFPEKKSA ISASELSLAD
GRDRPLRRLD PGMMPLPDTA AGLEWSSLVN AAKAYEVQRA VSLFSLNDPA LSPEIPPAHS
PVHSHLSLER GPQTPRATPT MSEESPLDLT GKVYQLEVML KQLHTDLQKE KQDKVVLQSE
VASLRQNNQR LQEESQAASE QLRKFAELFS REKKEL
