ID BICC1_MOUSE Reviewed; 977 AA.
AC Q99MQ1; Q6P6K3; Q8C286;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=Protein bicaudal C homolog 1;
DE Short=Bic-C;
GN Name=Bicc1;
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 TISSUE SPECIFICITY.
RC STRAIN=FVB/N-3;
RX PubMed=11231089; DOI=10.1016/s0925-4773(00)00568-2;
RA Wessely O., Tran U., Zakin L., De Robertis E.M.;
RT "Identification and expression of the mammalian homologue of Bicaudal-C.";
RL Mech. Dev. 101:267-270(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=NOD; TISSUE=Thymus;
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 MRNA] (ISOFORM 1).
RC TISSUE=Bone;
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 [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ANKS6.
RX PubMed=19324013; DOI=10.1016/j.bbrc.2009.03.113;
RA Stagner E.E., Bouvrette D.J., Cheng J., Bryda E.C.;
RT "The polycystic kidney disease-related proteins Bicc1 and SamCystin
RT interact.";
RL Biochem. Biophys. Res. Commun. 383:16-21(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-32; SER-45; SER-614
RP AND SER-681, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Kidney, 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).
RN [6]
RP INTERACTION WITH ANKS3.
RX PubMed=25671767; DOI=10.1038/ki.2015.17;
RA Yakulov T.A., Yasunaga T., Ramachandran H., Engel C., Mueller B., Hoff S.,
RA Dengjel J., Lienkamp S.S., Walz G.;
RT "Anks3 interacts with nephronophthisis proteins and is required for normal
RT renal development.";
RL Kidney Int. 87:1191-1200(2015).
CC -!- FUNCTION: Putative RNA-binding protein. May be involved in regulating
CC gene expression during embryonic development.
CC -!- SUBUNIT: Interacts (via KH domains) with ANKS6 (via SAM domain) in an
CC RNA-dependent manner. Interacts with ANKS3 (PubMed:25671767).
CC {ECO:0000269|PubMed:19324013, ECO:0000269|PubMed:25671767}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19324013}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99MQ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99MQ1-2; Sequence=VSP_021950, VSP_021951;
CC -!- TISSUE SPECIFICITY: In the adult, predominantly expressed in heart and
CC kidney. In 8 week old mice, expressed in growing primary oocytes and in
CC the stromal cells of the theca. {ECO:0000269|PubMed:11231089}.
CC -!- DEVELOPMENTAL STAGE: In the developing embryo, first detected at the
CC rostral tip of the primitive streak, Hensen's node, at the late streak
CC stage. At the late headfold stage, expression demarcates the layer of
CC the node from which definitive endoderm and midline mesoderm arises. At
CC 6-8 somite stage observed in the definitive endoderm. Strong expression
CC is detected in the caudal intestinal portal. At 12-15 somite stage is
CC still present in the hindgut, but transient expression is also seen in
CC tissues of neural and mesodermal origins. At 13 dpc present around all
CC sites of cartilage formation, such as cervical vertebral bodies, ribs
CC and Merckel's cartilage. Additionally, expressed in the derivatives of
CC the pleuroperitoneal membrane, the diaphragm and the pericardium, as
CC well as the mesenchyme of the developing lung. Expressed in both the
CC mesonephros and metanephros.
CC -!- SIMILARITY: Belongs to the BicC family. {ECO:0000305}.
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DR EMBL; AF319464; AAK27347.1; -; mRNA.
DR EMBL; AK089066; BAC40732.1; -; mRNA.
DR EMBL; BC062174; AAH62174.1; -; mRNA.
DR EMBL; BC111523; AAI11524.1; -; mRNA.
DR CCDS; CCDS23915.1; -. [Q99MQ1-1]
DR RefSeq; NP_113574.1; NM_031397.3. [Q99MQ1-1]
DR AlphaFoldDB; Q99MQ1; -.
DR SMR; Q99MQ1; -.
DR CORUM; Q99MQ1; -.
DR STRING; 10090.ENSMUSP00000123201; -.
DR iPTMnet; Q99MQ1; -.
DR PhosphoSitePlus; Q99MQ1; -.
DR jPOST; Q99MQ1; -.
DR MaxQB; Q99MQ1; -.
DR PaxDb; 10090-ENSMUSP00000123201; -.
DR ProteomicsDB; 273739; -. [Q99MQ1-1]
DR ProteomicsDB; 273740; -. [Q99MQ1-2]
DR Pumba; Q99MQ1; -.
DR Antibodypedia; 51885; 174 antibodies from 26 providers.
DR DNASU; 83675; -.
DR Ensembl; ENSMUST00000131445.8; ENSMUSP00000119137.2; ENSMUSG00000014329.15. [Q99MQ1-2]
DR Ensembl; ENSMUST00000143791.8; ENSMUSP00000123201.2; ENSMUSG00000014329.15. [Q99MQ1-1]
DR GeneID; 83675; -.
DR KEGG; mmu:83675; -.
DR UCSC; uc007fog.2; mouse. [Q99MQ1-1]
DR UCSC; uc033fpy.1; mouse. [Q99MQ1-2]
DR AGR; MGI:1933388; -.
DR CTD; 80114; -.
DR MGI; MGI:1933388; Bicc1.
DR VEuPathDB; HostDB:ENSMUSG00000014329; -.
DR eggNOG; KOG2208; Eukaryota.
DR eggNOG; KOG4374; Eukaryota.
DR GeneTree; ENSGT00940000156276; -.
DR HOGENOM; CLU_008040_0_0_1; -.
DR InParanoid; Q99MQ1; -.
DR OMA; PDNDTPY; -.
DR OrthoDB; 2906718at2759; -.
DR PhylomeDB; Q99MQ1; -.
DR TreeFam; TF323767; -.
DR BioGRID-ORCS; 83675; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Bicc1; mouse.
DR PRO; PR:Q99MQ1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q99MQ1; Protein.
DR Bgee; ENSMUSG00000014329; Expressed in efferent duct and 230 other cell types or tissues.
DR ExpressionAtlas; Q99MQ1; baseline and differential.
DR Genevisible; Q99MQ1; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISA:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR CDD; cd22420; KH-I_BICC1_rpt1; 1.
DR CDD; cd22421; KH-I_BICC1_rpt2; 1.
DR CDD; cd22422; KH-I_BICC1_rpt3; 1.
DR CDD; cd09520; SAM_BICC1; 1.
DR Gene3D; 3.30.310.270; -; 2.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR047549; BICC1_KH-I_rpt1.
DR InterPro; IPR047554; BICC1_KH-I_rpt2.
DR InterPro; IPR047553; BICC1_KH-I_rpt3.
DR InterPro; IPR037974; BICC1_SAM_dom.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR10627:SF78; PROTEIN BICAUDAL C HOMOLOG 1; 1.
DR PANTHER; PTHR10627; SCP160; 1.
DR Pfam; PF00013; KH_1; 2.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00322; KH; 3.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 3.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50084; KH_TYPE_1; 2.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Developmental protein;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..977
FT /note="Protein bicaudal C homolog 1"
FT /id="PRO_0000267715"
FT DOMAIN 134..201
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 286..350
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 875..938
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 400
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H694"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021950"
FT VAR_SEQ 934..977
FT /note="ELSKNRRKLFEPPNASCTSFLEGGASGRLPRQYHSDIASVSGRW -> VCDS
FT VQIRNKILRAARIL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021951"
FT CONFLICT 276
FT /note="H -> R (in Ref. 2; BAC40732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 977 AA; 105037 MW; 3A5A7B7F2CA84918 CRC64;
MASQSEPGYL AAAQSDPGSN SERSTDSPVA GSEDDLVAAA PLLHSPEWSE ERFRVDRKKL
EAMLQAAAEG KGRSGEDFFQ KIMEETNTQI AWPSKLKIGA KSKKDPHIKV SGKKEDVKEA
KEMIMSVLDT KSNRVTLKMD VSHTEHSHVI GKGGNNIKKV MEDTGCHIHF PDSNRNNQAE
KSNQVSIAGQ PAGVESARAR IRELLPLVLM FELPIAGILQ PVPDPNTPSI QHISQTYSVS
VSFKQRSRMY GATVTVRGSQ NNTNAVKEGT AMLLEHLAGS LASAIPVSTQ LDIAAQHHLF
MMGRNGSNVK HIMQRTGAQI HFPDPSNPQK KSTVYLQGTI ESVCLARQYL MGCLPLVLMF
DMKEDIEVDP QVIAQLMEQL DVFISIKPKP KQPSKSVIVK SVERNALNMY EARKCLLGLE
SSGVSIATSL SPASCPAGLA CPSLDILASA GLGLTGLGLL GPTTLSLNTS ATPNSLLNAL
NTSVSPLQSS SSGTPSPTLW APPIANTASA TGFSTIPHLM LPSTAQATLT NILLSGVPTY
GHTAPSPPPG LTPVDVHINS MQTEGKNISA SINGHVQPAN MKYGPLSTSS LGEKVLSSNH
GDPSMQTAGP EQASPKSNSV EGCNDAFVEV GMPRSPSHSG NAGDLKQMLG ASKVSCAKRQ
TVELLQGTKN SHLHGTDRLL SDPELSATES PLADKKAPGS ERAAERAAAA QQKSERARLA
SQPTYVHMQA FDYEQKKLLA TKAMLKKPVV TEVRTPTNTW SGLGFSKSMP AETIKELRRA
NHVSYKPTMT TAYEGSSLSL SRSSSREHLA SGSESDNWRD RNGIGPMGHS EFSAPIGSPK
RKQNKSREHY LSSSNYMDCI SSLTGSNGCN LNSCFKGSDL PELFSKLGLG KYTDVFQQQE
IDLQTFLTLT DQDLKELGIT TFGARRKMLL AISELSKNRR KLFEPPNASC TSFLEGGASG
RLPRQYHSDI ASVSGRW
//
