CASS4_MOUSE
ID CASS4_MOUSE Reviewed; 804 AA.
AC Q08EC4; A1L397; Q08EC3; Q3TCH3;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cas scaffolding protein family member 4 {ECO:0000312|EMBL:AAI17859.1};
GN Name=Cass4 {ECO:0000312|MGI:MGI:2444482};
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] {ECO:0000305, ECO:0000312|EMBL:BAE41983.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=NOD {ECO:0000312|EMBL:BAE41983.1};
RC TISSUE=Dendritic cell {ECO:0000312|EMBL:BAE41983.1};
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 [2]
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAI17859.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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: Docking protein that plays a role in tyrosine kinase-based
CC signaling related to cell adhesion and cell spreading. Regulates
CC PTK2/FAK1 activity, focal adhesion integrity, and cell spreading (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via SH3 domain) with PTK2/FAK1 (via C-terminus).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9NQ75}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q9NQ75}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:15489334};
CC IsoId=Q08EC4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q08EC4-2; Sequence=VSP_052948, VSP_052950;
CC Name=3 {ECO:0000269|PubMed:16141072};
CC IsoId=Q08EC4-3; Sequence=VSP_052949, VSP_052951;
CC -!- PTM: Phosphorylated on tyrosines by SRC.
CC {ECO:0000250|UniProtKB:Q9NQ75}.
CC -!- SIMILARITY: Belongs to the CAS family. {ECO:0000255}.
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DR EMBL; AK170726; BAE41983.1; -; mRNA.
DR EMBL; AL833787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117858; AAI17859.1; -; mRNA.
DR EMBL; BC117859; AAI17860.1; -; mRNA.
DR EMBL; BC129975; AAI29976.1; -; mRNA.
DR EMBL; BC129976; AAI29977.1; -; mRNA.
DR CCDS; CCDS38347.1; -. [Q08EC4-1]
DR CCDS; CCDS89589.1; -. [Q08EC4-2]
DR RefSeq; NP_001074289.1; NM_001080820.2. [Q08EC4-1]
DR RefSeq; NP_001263351.1; NM_001276422.1. [Q08EC4-2]
DR RefSeq; NP_001263352.1; NM_001276423.1.
DR AlphaFoldDB; Q08EC4; -.
DR SMR; Q08EC4; -.
DR BioGRID; 236200; 3.
DR STRING; 10090.ENSMUSP00000104764; -.
DR iPTMnet; Q08EC4; -.
DR PhosphoSitePlus; Q08EC4; -.
DR EPD; Q08EC4; -.
DR MaxQB; Q08EC4; -.
DR PaxDb; Q08EC4; -.
DR PeptideAtlas; Q08EC4; -.
DR PRIDE; Q08EC4; -.
DR ProteomicsDB; 279917; -. [Q08EC4-1]
DR ProteomicsDB; 279918; -. [Q08EC4-2]
DR ProteomicsDB; 279919; -. [Q08EC4-3]
DR Antibodypedia; 2766; 76 antibodies from 19 providers.
DR DNASU; 320664; -.
DR Ensembl; ENSMUST00000099061; ENSMUSP00000096660; ENSMUSG00000074570. [Q08EC4-3]
DR Ensembl; ENSMUST00000109136; ENSMUSP00000104764; ENSMUSG00000074570. [Q08EC4-1]
DR Ensembl; ENSMUST00000228775; ENSMUSP00000154073; ENSMUSG00000074570. [Q08EC4-2]
DR GeneID; 320664; -.
DR KEGG; mmu:320664; -.
DR UCSC; uc008ocr.1; mouse. [Q08EC4-3]
DR UCSC; uc008ocs.2; mouse. [Q08EC4-1]
DR UCSC; uc008oct.2; mouse. [Q08EC4-2]
DR CTD; 57091; -.
DR MGI; MGI:2444482; Cass4.
DR VEuPathDB; HostDB:ENSMUSG00000074570; -.
DR eggNOG; ENOG502QUJM; Eukaryota.
DR GeneTree; ENSGT00950000183008; -.
DR InParanoid; Q08EC4; -.
DR OMA; RFASMVI; -.
DR OrthoDB; 1086228at2759; -.
DR PhylomeDB; Q08EC4; -.
DR TreeFam; TF328782; -.
DR BioGRID-ORCS; 320664; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Cass4; mouse.
DR PRO; PR:Q08EC4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q08EC4; protein.
DR Bgee; ENSMUSG00000074570; Expressed in left lung lobe and 44 other tissues.
DR ExpressionAtlas; Q08EC4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0090527; P:actin filament reorganization; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd12000; SH3_CASS4; 1.
DR Gene3D; 1.20.120.830; -; 1.
DR InterPro; IPR021901; CAS_C.
DR InterPro; IPR037362; CAS_fam.
DR InterPro; IPR035512; CASS4.
DR InterPro; IPR035744; CASS4_SH3.
DR InterPro; IPR014928; Serine_rich_dom.
DR InterPro; IPR038319; Serine_rich_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10654; PTHR10654; 1.
DR PANTHER; PTHR10654:SF19; PTHR10654:SF19; 1.
DR Pfam; PF12026; CAS_C; 1.
DR Pfam; PF08824; Serine_rich; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..804
FT /note="Cas scaffolding protein family member 4"
FT /id="PRO_0000351205"
FT DOMAIN 11..73
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 369..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ75"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 212
FT /note="Q -> QAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052948"
FT VAR_SEQ 643..685
FT /note="QSPNLQEKGKPTMEGKSNRNPDFHGMSPPPLTSPSPSGQNTER -> VSQGD
FT KQYTGDFICYLNWSSLRQMLASCACRNVHLHVHGEAIG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052949"
FT VAR_SEQ 643..668
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052950"
FT VAR_SEQ 686..804
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052951"
SQ SEQUENCE 804 AA; 88621 MW; AAC670C0ACA5FAD9 CRC64;
MRGTSIREGA PKTLLARALY DNHADCSDEL AFSRGDILTI VEQNVPESEG WWRCLLHGRQ
GLAPANRLQV LRETPADRPC PLLPRGPDTD LTSSGAPYQV QDLISPPPQG PVYEPMRSWV
EGPSPATAQV YELPESPSSA RIICEKTLSF PKQALSVLPR PTRASLPTLP SQVYDVPVQR
QGFSTLERLE KQQFYDIPTS SQKALLHSST SQGRDVTLAP TMAFRQGGGY NPLSSPQKSE
RIHDTPVLLE KADVRNVSMT SFTKDSGSRA IPGSSAVHTG AVALSPQLGN TVQRKNSLPE
EPTYAFPTSR DPLPSDAGGS YKVPSRFLIP RVEQQNTMPN IYDTPKAMQG VSHNAPKAMQ
GVSLAGKELE RGREAPENSP WISGQTSFLS PDSDRLSVAS SDSRASVVSS CSSISMDSSS
GSSSEDSVKE LWMDVDFAKE TAVSLQHKVA SSAAGLLLFV SRTWRFKDSL ETNIHRIRRA
ADHVEESVRE FLDFAQGVGG TACNLTDSYL QARIRDQLQT ISSSYQTLLD AKGSLDRCNW
SLEVLVTDKV QNSLDDLERF VATARIVPED VKRFTSIVIA NGKLLFKQNC EKGEMDLKCE
RCIRPPQRET ESYQESSPFD RQPTTEHSFE LARKNRVNVC WQQSPNLQEK GKPTMEGKSN
RNPDFHGMSP PPLTSPSPSG QNTERKIHLS KHSRLYFGAL FKAISVFASS LSNGQPPEVF
ITQSKLVITV GQKLVDTLCS ETQEKDERNE ILCGSSHLCG LLKDLALATK SAVIQYPSPS
ALSLLQSEVE RLEHHSRKFR DTLE
