SAPC2_MOUSE
ID SAPC2_MOUSE Reviewed; 391 AA.
AC Q9D818; A2AJ17; Q3TL89; Q3TP90; Q3TQ24; Q6NS42;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Suppressor APC domain-containing protein 2 {ECO:0000305};
DE AltName: Full=Protein Ang;
GN Name=Sapcd2 {ECO:0000312|MGI:MGI:1919330};
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] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=15567712; DOI=10.1016/j.modgep.2004.08.007;
RA Murata T., Furushima K., Hirano M., Kiyonari H., Nakamura M., Suda Y.,
RA Aizawa S.;
RT "Ang is a novel gene expressed in early neuroectoderm, but its null mutant
RT exhibits no obvious phenotype.";
RL Gene Expr. Patterns 5:171-178(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Lung, and Small intestine;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=26766442; DOI=10.1016/j.devcel.2015.12.016;
RA Chiu C.W., Monat C., Robitaille M., Lacomme M., Daulat A.M., Macleod G.,
RA McNeill H., Cayouette M., Angers S.;
RT "SAPCD2 controls spindle orientation and asymmetric divisions by negatively
RT regulating the Galphai-LGN-NuMA ternary complex.";
RL Dev. Cell 36:50-62(2016).
CC -!- FUNCTION: Plays a role in planar mitotic spindle orientation in retinal
CC progenitor cells (RPCs) and promotes the production of symmetric
CC terminal divisions (PubMed:26766442). Negatively regulates the mitotic
CC apical cortex localization of GPSM2 (By similarity). Involved also in
CC positive regulation of cell proliferation and tumor cell growth (By
CC similarity). {ECO:0000250|UniProtKB:Q86UD0,
CC ECO:0000269|PubMed:26766442}.
CC -!- SUBUNIT: Interacts with a spindle orientation complex at least composed
CC of GNAI1, GPSM2 and NUMA1. Interacts with GPSM2 (via TPR motifs); this
CC interaction is required to prevent GPSM2 anchoring at the mitotic
CC apical cortex and is inhibited in presence of NUMA1 in a dose dependent
CC manner. Interacts with PARD3. {ECO:0000250|UniProtKB:Q86UD0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86UD0}. Nucleus
CC {ECO:0000250|UniProtKB:Q86UD0}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q86UD0}. Apical cell membrane
CC {ECO:0000269|PubMed:26766442}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q86UD0}. Note=Localized at the apical membrane
CC during the M phase (PubMed:26766442). In horizontally retinal
CC progenitor dividing cells, localized at the pole cortical region from
CC prophase to telophase cells (PubMed:26766442). In vertically retinal
CC progenitor dividing cells, not detected at the pole cortical region at
CC any stage of mitosis (PubMed:26766442). {ECO:0000269|PubMed:26766442}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9D818-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D818-2; Sequence=VSP_025112;
CC Name=3;
CC IsoId=Q9D818-3; Sequence=VSP_025113;
CC -!- TISSUE SPECIFICITY: Expressed in the retina (PubMed:26766442).
CC Expressed in retinal progenitor cells and newly differentiated neurons
CC but not in mature retinal cells (at protein level) (PubMed:26766442).
CC {ECO:0000269|PubMed:26766442}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryonic retina from 14 to 17
CC dpc (at protein level) (PubMed:26766442). Expressed throughout
CC neuroectoderm at 7.5 dpc (PubMed:15567712). The expression increases in
CC rostral brain and caudal neuropore regions and decreases in hindbrain
CC and spinal cord regions (PubMed:15567712). At 12.5 dpc the expression
CC is found in undifferentiated neuroepithelium in ventricular zone,
CC dorsal root ganglia and several non-neural tissues (PubMed:15567712).
CC {ECO:0000269|PubMed:15567712, ECO:0000269|PubMed:26766442}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH70477.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB197927; BAD86554.1; -; mRNA.
DR EMBL; AK008577; BAB25756.1; -; mRNA.
DR EMBL; AK163973; BAE37561.1; -; mRNA.
DR EMBL; AK164615; BAE37847.1; -; mRNA.
DR EMBL; AK166625; BAE38903.1; -; mRNA.
DR EMBL; AL732557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC070477; AAH70477.1; ALT_INIT; mRNA.
DR CCDS; CCDS38073.1; -. [Q9D818-2]
DR CCDS; CCDS70999.1; -. [Q9D818-1]
DR RefSeq; NP_001074554.1; NM_001081085.2. [Q9D818-2]
DR RefSeq; NP_001277336.1; NM_001290407.1. [Q9D818-1]
DR RefSeq; XP_006498423.1; XM_006498360.3. [Q9D818-3]
DR AlphaFoldDB; Q9D818; -.
DR SMR; Q9D818; -.
DR iPTMnet; Q9D818; -.
DR PhosphoSitePlus; Q9D818; -.
DR EPD; Q9D818; -.
DR jPOST; Q9D818; -.
DR MaxQB; Q9D818; -.
DR PeptideAtlas; Q9D818; -.
DR PRIDE; Q9D818; -.
DR ProteomicsDB; 256593; -. [Q9D818-1]
DR ProteomicsDB; 256594; -. [Q9D818-2]
DR ProteomicsDB; 256595; -. [Q9D818-3]
DR Antibodypedia; 52195; 57 antibodies from 14 providers.
DR DNASU; 72080; -.
DR Ensembl; ENSMUST00000028329; ENSMUSP00000028329; ENSMUSG00000026955. [Q9D818-2]
DR Ensembl; ENSMUST00000100323; ENSMUSP00000097898; ENSMUSG00000026955. [Q9D818-3]
DR Ensembl; ENSMUST00000114293; ENSMUSP00000109932; ENSMUSG00000026955. [Q9D818-1]
DR GeneID; 72080; -.
DR KEGG; mmu:72080; -.
DR UCSC; uc008irt.2; mouse. [Q9D818-3]
DR UCSC; uc008iru.2; mouse. [Q9D818-2]
DR UCSC; uc008irv.2; mouse. [Q9D818-1]
DR CTD; 89958; -.
DR MGI; MGI:1919330; Sapcd2.
DR VEuPathDB; HostDB:ENSMUSG00000026955; -.
DR eggNOG; ENOG502QUJT; Eukaryota.
DR GeneTree; ENSGT00390000008072; -.
DR HOGENOM; CLU_024930_0_0_1; -.
DR InParanoid; Q9D818; -.
DR OMA; HNNHEMS; -.
DR OrthoDB; 1453181at2759; -.
DR PhylomeDB; Q9D818; -.
DR TreeFam; TF324086; -.
DR BioGRID-ORCS; 72080; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Sapcd2; mouse.
DR PRO; PR:Q9D818; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D818; protein.
DR Bgee; ENSMUSG00000026955; Expressed in ventricular zone and 124 other tissues.
DR Genevisible; Q9D818; MM.
DR GO; GO:0045179; C:apical cortex; IDA:UniProtKB.
DR GO; GO:0043296; C:apical junction complex; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:1904777; P:negative regulation of protein localization to cell cortex; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0090175; P:regulation of establishment of planar polarity; IMP:UniProtKB.
DR GO; GO:0098725; P:symmetric cell division; IMP:UniProtKB.
DR InterPro; IPR026828; Suppressor_APCD_1/2.
DR PANTHER; PTHR14907; PTHR14907; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cell junction;
KW Cell membrane; Coiled coil; Cytoplasm; Membrane; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Tight junction.
FT CHAIN 1..391
FT /note="Suppressor APC domain-containing protein 2"
FT /id="PRO_0000286597"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 226..277
FT /evidence="ECO:0000255"
FT COILED 340..381
FT /evidence="ECO:0000255"
FT MOD_RES 218
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86UD0"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UD0"
FT VAR_SEQ 189
FT /note="L -> LGSSQCDTLQRQPGLLLHPGGRGGSTGAPSTSAEE (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025112"
FT VAR_SEQ 313..348
FT /note="ALPSSSLGPLGPPSPSTPVWQQQTILMLKEQNRLLT -> VSALEAAWHPLS
FT LFWMLCQERSGSLCTSTGSAFVLFRAPGPSLTLNSSLAATDHPHAERTEPASHSGEVWE
FT DGAGAGGPANPDRLPACSPA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025113"
FT CONFLICT 367
FT /note="A -> T (in Ref. 2; BAE38903)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 42780 MW; 7743BBD7125E4735 CRC64;
MAVAAMAERG RLSHAAPAPS TEGLPRAFLQ SLRTLFDILD DRQRGYVHLR EIESRWQGAD
ARELPCGVLE GLRQVAPANG YLTFERFVAG LRTSLLKADG GQRDQARVAA RPGDQSSLQQ
RLMFAPADEP RTVLERKPLP LSACPASGGP SGTSRNPELL CVPVEAASCP TETERPLSKA
LEQIPSADLG AAACKTLGKG TGEARQAPRA RGERRRHTIT NGVDCSLLKQ MKELDQEQEV
LLQGLEMMAR GRDWYQQQLQ RVQERQRRLS QSRAAADFGA EGSPRPLGRL LPKVQEVARC
LGELLTAACS GRALPSSSLG PLGPPSPSTP VWQQQTILML KEQNRLLTQE VTDKSERITQ
LEQEKSALIK QLFEARALSQ QDSGPLDSTF I
