SDCG8_MOUSE
ID SDCG8_MOUSE Reviewed; 717 AA.
AC Q80UF4;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Serologically defined colon cancer antigen 8 homolog;
DE AltName: Full=Centrosomal colon cancer autoantigen protein;
DE Short=mCCCAP;
GN Name=Sdccag8; Synonyms=Cccap;
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], SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=12559564; DOI=10.1016/s0378-1119(02)01141-1;
RA Kenedy A.A., Cohen K.J., Loveys D.A., Kato G.J., Dang C.V.;
RT "Identification and characterization of the novel centrosome-associated
RT protein CCCAP.";
RL Gene 303:35-46(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Pituitary;
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 FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20835237; DOI=10.1038/ng.662;
RA Otto E.A., Hurd T.W., Airik R., Chaki M., Zhou W., Stoetzel C., Patil S.B.,
RA Levy S., Ghosh A.K., Murga-Zamalloa C.A., van Reeuwijk J., Letteboer S.J.,
RA Sang L., Giles R.H., Liu Q., Coene K.L., Estrada-Cuzcano A., Collin R.W.,
RA McLaughlin H.M., Held S., Kasanuki J.M., Ramaswami G., Conte J., Lopez I.,
RA Washburn J., Macdonald J., Hu J., Yamashita Y., Maher E.R.,
RA Guay-Woodford L.M., Neumann H.P., Obermuller N., Koenekoop R.K.,
RA Bergmann C., Bei X., Lewis R.A., Katsanis N., Lopes V., Williams D.S.,
RA Lyons R.H., Dang C.V., Brito D.A., Dias M.B., Zhang X., Cavalcoli J.D.,
RA Nurnberg G., Nurnberg P., Pierce E.A., Jackson P.K., Antignac C.,
RA Saunier S., Roepman R., Dollfus H., Khanna H., Hildebrandt F.;
RT "Candidate exome capture identifies mutation of SDCCAG8 as the cause of a
RT retinal-renal ciliopathy.";
RL Nat. Genet. 42:840-850(2010).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27224062; DOI=10.1371/journal.pone.0156081;
RA Airik R., Schueler M., Airik M., Cho J., Ulanowicz K.A., Porath J.D.,
RA Hurd T.W., Bekker-Jensen S., Schroeder J.M., Andersen J.S., Hildebrandt F.;
RT "SDCCAG8 interacts with RAB effector proteins RABEP2 and ERC1 and is
RT required for Hedgehog Signaling.";
RL PLoS ONE 11:E0156081-E0156081(2016).
CC -!- FUNCTION: Plays a role in the establishment of cell polarity and
CC epithelial lumen formation (PubMed:20835237). Also plays an essential
CC role in ciliogenesis and subsequent Hedgehog signaling pathway that
CC requires the presence of intact primary cilia for pathway activation.
CC Mechanistically, interacts with and mediates RABEP2 centrosomal
CC localization which is critical for ciliogenesis (PubMed:27224062).
CC {ECO:0000269|PubMed:20835237, ECO:0000269|PubMed:27224062}.
CC -!- SUBUNIT: Homodimer (PubMed:12559564). Interacts with OFD1; the
CC interaction is direct (By similarity). Interacts with FAM161A (By
CC similarity). Interacts with RABEP2, ERC1 and CEP131 (By similarity).
CC {ECO:0000250|UniProtKB:Q86SQ7, ECO:0000269|PubMed:12559564}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:12559564,
CC ECO:0000269|PubMed:20835237}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q86SQ7}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q86SQ7}. Cell junction
CC {ECO:0000250|UniProtKB:Q86SQ7}. Note=Located at the distal ends of both
CC centrioles and colocalizes to centrosomes throughout the cell cycle.
CC {ECO:0000250|UniProtKB:Q86SQ7}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, spleen, brain, heart
CC and muscle. Expressed in photoreceptor cells of the retina.
CC {ECO:0000269|PubMed:12559564, ECO:0000269|PubMed:20835237}.
CC -!- DISRUPTION PHENOTYPE: In renal epithelial cells gene knockdown results
CC in the formation of spheroids with architectural defects characterized
CC by disturbed localization of beta-catenin (CTNNB1) at the basolateral
CC membrane, fewer tight junctions and an irregular lumen
CC (PubMed:20835237). SDCCAG8-deficient mice display developmental bone
CC malformations with rib cage abnormalities.
CC {ECO:0000269|PubMed:20835237, ECO:0000269|PubMed:27224062}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF250729; AAO27828.1; -; mRNA.
DR EMBL; AK132316; BAE21100.1; -; mRNA.
DR EMBL; AK133622; BAE21753.1; -; mRNA.
DR CCDS; CCDS35798.1; -.
DR RefSeq; NP_084032.1; NM_029756.3.
DR AlphaFoldDB; Q80UF4; -.
DR SMR; Q80UF4; -.
DR BioGRID; 218334; 25.
DR IntAct; Q80UF4; 24.
DR STRING; 10090.ENSMUSP00000027785; -.
DR iPTMnet; Q80UF4; -.
DR PhosphoSitePlus; Q80UF4; -.
DR EPD; Q80UF4; -.
DR MaxQB; Q80UF4; -.
DR PaxDb; Q80UF4; -.
DR PRIDE; Q80UF4; -.
DR ProteomicsDB; 256940; -.
DR Antibodypedia; 34709; 244 antibodies from 33 providers.
DR Ensembl; ENSMUST00000027785; ENSMUSP00000027785; ENSMUSG00000026504.
DR GeneID; 76816; -.
DR KEGG; mmu:76816; -.
DR UCSC; uc007duj.2; mouse.
DR CTD; 10806; -.
DR MGI; MGI:1924066; Sdccag8.
DR VEuPathDB; HostDB:ENSMUSG00000026504; -.
DR eggNOG; ENOG502R5XE; Eukaryota.
DR GeneTree; ENSGT00730000111198; -.
DR HOGENOM; CLU_024506_0_0_1; -.
DR InParanoid; Q80UF4; -.
DR OMA; SQEKMYT; -.
DR OrthoDB; 654910at2759; -.
DR PhylomeDB; Q80UF4; -.
DR TreeFam; TF325472; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 76816; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Sdccag8; mouse.
DR PRO; PR:Q80UF4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q80UF4; protein.
DR Bgee; ENSMUSG00000026504; Expressed in floor plate of midbrain and 223 other tissues.
DR ExpressionAtlas; Q80UF4; baseline and differential.
DR Genevisible; Q80UF4; MM.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0034451; C:centriolar satellite; IDA:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0097733; C:photoreceptor cell cilium; IDA:MGI.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; IEA:InterPro.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0035148; P:tube formation; IMP:UniProtKB.
DR InterPro; IPR031887; SDCCAG8.
DR PANTHER; PTHR34343; PTHR34343; 1.
DR Pfam; PF15964; CCCAP; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell projection; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..717
FT /note="Serologically defined colon cancer antigen 8
FT homolog"
FT /id="PRO_0000076311"
FT REGION 84..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..717
FT /note="Sufficient for homodimerization"
FT COILED 129..168
FT /evidence="ECO:0000255"
FT COILED 221..278
FT /evidence="ECO:0000255"
FT COILED 352..590
FT /evidence="ECO:0000255"
FT COILED 622..712
FT /evidence="ECO:0000255"
FT COMPBIAS 89..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86SQ7"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86SQ7"
SQ SEQUENCE 717 AA; 82979 MW; C9F69DBFB3DCD59D CRC64;
MAKSPGNSTL EDSLGQYQRS LRERANRSIH QLKCALREVD VTVEEDALDP STSINVENED
TGVAWHELQH SHAVNQLKAL LRQQTNKENE TSPPRRRKLS PSRPSECDDG SMPTMHNLVP
IINDQSQYIH HLEAEVKFCK DELSGMKNRV QVVVLENERL QQELKSQRPE ETLREQTFLD
ASGNMQNSWI MTREDSRVDE AAKRPFSHGD AETGKTASTG DANKWKLELE RLKLTYEAKT
DLLESQLMLL RKDLAEYQKT CEDLKERLKH KESLLAASAS SRVGGLCLKC AQHEAVLSQT
HSNVHIQTIE RLTKERDDLM SVLVSVRSSL AEAQKRETSA YEQVKHAVQM TEEANFEKTK
ALIQCEQLKS ELERQTERLE KELASQQEKR AVEKEMIKKE VAREREDAES KMLILSQNIA
KLEAQVEKVT REKTAAVSHL EEIQNHVASQ EMDVTKVCGE MRFQLNKTKM EKDEVEKEHR
EYKAKSHKDL EMKVQEIEKL RLELSESEQH VEQEQQKAAR ARQECLRVTE LLGEAERQLH
LTRLEKDSIQ QSFSNEAKAQ ALQAQQREQE LTQKIQQMET QHDKTESEQY LLLTSQNTFL
TKLKEECCLL AKKLEKVSLK SRSQIVRLSQ EKRYLCDKLE KLQKRNDELE EQCIQHGRVH
ETMKERLRQL DKHGQATAQQ LVQLLNKQNQ LLLERQNLSE EVARLRAQLP SMPQSDC
