ID   CRKL_MOUSE              Reviewed;         303 AA.
AC   P47941; Q3TQ18; Q8BGC5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   24-JAN-2024, entry version 185.
DE   RecName: Full=Crk-like protein;
GN   Name=Crkl; Synonyms=Crkol;
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].
RC   STRAIN=C57BL X CBA; TISSUE=Placenta;
RX   PubMed=7478571;
RA   de Jong R.L., Haataja L., Voncken J.W., Heisterkamp N., Groffen J.;
RT   "Tyrosine phosphorylation of murine Crkl.";
RL   Oncogene 11:1469-1474(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head, and Embryonic heart;
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   INTERACTION WITH INPP5D.
RX   PubMed=11031258; DOI=10.1074/jbc.m006250200;
RA   Sattler M., Verma S., Pride Y.B., Salgia R., Rohrschneider L.R.,
RA   Griffin J.D.;
RT   "SHIP1, an SH2 domain containing polyinositol-5-phosphatase, regulates
RT   migration through two critical tyrosine residues and forms a novel
RT   signaling complex with DOK1 and CRKL.";
RL   J. Biol. Chem. 276:2451-2458(2001).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   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).
CC   -!- FUNCTION: May mediate the transduction of intracellular signals.
CC   -!- SUBUNIT: Interacts with DOCK2 and EPOR. Interacts with phosphorylated
CC       CBLB and IRS4 (By similarity). Interacts with INPP5D/SHIP1
CC       (PubMed:11031258). Interacts with BCAR1/CAS and NEDD9/HEF1 (By
CC       similarity). {ECO:0000250|UniProtKB:P46109,
CC       ECO:0000269|PubMed:11031258}.
CC   -!- PTM: Phosphorylated on tyrosine. Phosphorylation is prominent during
CC       early development, but decreases at later embryonic stages and in
CC       newborn mice.
CC   -!- SIMILARITY: Belongs to the CRK family. {ECO:0000305}.
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DR   EMBL; X90648; CAA62220.1; -; mRNA.
DR   EMBL; AK048641; BAC33406.1; -; mRNA.
DR   EMBL; AK052315; BAC34933.1; -; mRNA.
DR   EMBL; AK163981; BAE37567.1; -; mRNA.
DR   CCDS; CCDS28002.1; -.
DR   PIR; S58352; S58352.
DR   RefSeq; NP_001264160.1; NM_001277231.1.
DR   RefSeq; NP_031790.2; NM_007764.5.
DR   AlphaFoldDB; P47941; -.
DR   BMRB; P47941; -.
DR   SMR; P47941; -.
DR   BioGRID; 198888; 28.
DR   CORUM; P47941; -.
DR   IntAct; P47941; 9.
DR   MINT; P47941; -.
DR   STRING; 10090.ENSMUSP00000006293; -.
DR   GlyGen; P47941; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P47941; -.
DR   PhosphoSitePlus; P47941; -.
DR   SwissPalm; P47941; -.
DR   REPRODUCTION-2DPAGE; IPI00113362; -.
DR   EPD; P47941; -.
DR   jPOST; P47941; -.
DR   MaxQB; P47941; -.
DR   PaxDb; 10090-ENSMUSP00000006293; -.
DR   ProteomicsDB; 278035; -.
DR   Pumba; P47941; -.
DR   Antibodypedia; 255; 807 antibodies from 39 providers.
DR   DNASU; 12929; -.
DR   Ensembl; ENSMUST00000006293.5; ENSMUSP00000006293.4; ENSMUSG00000006134.5.
DR   GeneID; 12929; -.
DR   KEGG; mmu:12929; -.
DR   UCSC; uc007ykv.2; mouse.
DR   AGR; MGI:104686; -.
DR   CTD; 1399; -.
DR   MGI; MGI:104686; Crkl.
DR   VEuPathDB; HostDB:ENSMUSG00000006134; -.
DR   eggNOG; KOG4792; Eukaryota.
DR   GeneTree; ENSGT00820000127055; -.
DR   HOGENOM; CLU_060542_0_1_1; -.
DR   InParanoid; P47941; -.
DR   OMA; WYVGPLS; -.
DR   OrthoDB; 2900795at2759; -.
DR   PhylomeDB; P47941; -.
DR   TreeFam; TF321436; -.
DR   Reactome; R-MMU-170968; Frs2-mediated activation.
DR   Reactome; R-MMU-186763; Downstream signal transduction.
DR   Reactome; R-MMU-8875555; MET activates RAP1 and RAC1.
DR   Reactome; R-MMU-8875656; MET receptor recycling.
DR   Reactome; R-MMU-9027284; Erythropoietin activates RAS.
DR   Reactome; R-MMU-912631; Regulation of signaling by CBL.
DR   BioGRID-ORCS; 12929; 8 hits in 79 CRISPR screens.
DR   ChiTaRS; Crkl; mouse.
DR   PRO; PR:P47941; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; P47941; Protein.
DR   Bgee; ENSMUSG00000006134; Expressed in rostral migratory stream and 274 other cell types or tissues.
DR   ExpressionAtlas; P47941; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0098890; C:extrinsic component of postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR   GO; GO:0035591; F:signaling adaptor activity; IGI:MGI.
DR   GO; GO:0095500; P:acetylcholine receptor signaling pathway; IGI:MGI.
DR   GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IGI:MGI.
DR   GO; GO:0001783; P:B cell apoptotic process; IMP:MGI.
DR   GO; GO:0001568; P:blood vessel development; IGI:MGI.
DR   GO; GO:0060326; P:cell chemotaxis; IGI:MGI.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
DR   GO; GO:0098749; P:cerebellar neuron development; IGI:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IGI:MGI.
DR   GO; GO:0160093; P:chordate pharynx development; IMP:MGI.
DR   GO; GO:1904888; P:cranial skeletal system development; IMP:MGI.
DR   GO; GO:0016358; P:dendrite development; IGI:MGI.
DR   GO; GO:0086100; P:endothelin receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007167; P:enzyme-linked receptor protein signaling pathway; IDA:MGI.
DR   GO; GO:0030010; P:establishment of cell polarity; IGI:MGI.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IGI:MGI.
DR   GO; GO:0035685; P:helper T cell diapedesis; IGI:MGI.
DR   GO; GO:0021766; P:hippocampus development; IGI:MGI.
DR   GO; GO:0006629; P:lipid metabolic process; IGI:MGI.
DR   GO; GO:0008584; P:male gonad development; IMP:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
DR   GO; GO:0060017; P:parathyroid gland development; IGI:MGI.
DR   GO; GO:0007389; P:pattern specification process; IGI:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:MGI.
DR   GO; GO:1903977; P:positive regulation of glial cell migration; ISO:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0035022; P:positive regulation of Rac protein signal transduction; IMP:MGI.
DR   GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IDA:MGI.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR   GO; GO:0098698; P:postsynaptic specialization assembly; IDA:SynGO.
DR   GO; GO:0038026; P:reelin-mediated signaling pathway; IMP:MGI.
DR   GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IGI:MGI.
DR   GO; GO:0001558; P:regulation of cell growth; IDA:MGI.
DR   GO; GO:0050773; P:regulation of dendrite development; IGI:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0002685; P:regulation of leukocyte migration; IGI:MGI.
DR   GO; GO:1904393; P:regulation of skeletal muscle acetylcholine-gated channel clustering; IGI:MGI.
DR   GO; GO:2000404; P:regulation of T cell migration; IGI:MGI.
DR   GO; GO:0071774; P:response to fibroblast growth factor; IMP:MGI.
DR   GO; GO:0048384; P:retinoic acid receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007338; P:single fertilization; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IDA:MGI.
DR   GO; GO:0048538; P:thymus development; IGI:MGI.
DR   GO; GO:0001655; P:urogenital system development; IMP:MGI.
DR   CDD; cd09926; SH2_CRK_like; 1.
DR   CDD; cd11759; SH3_CRK_C; 1.
DR   CDD; cd11758; SH3_CRK_N; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR035458; CRK_SH3_C.
DR   InterPro; IPR035457; CRK_SH3_N.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR19969:SF20; CRK-LIKE PROTEIN; 1.
DR   PANTHER; PTHR19969; SH2-SH3 ADAPTOR PROTEIN-RELATED; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 2.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 2.
DR   Genevisible; P47941; MM.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome; Repeat; SH2 domain; SH3 domain.
FT   CHAIN           1..303
FT                   /note="Crk-like protein"
FT                   /id="PRO_0000079348"
FT   DOMAIN          14..102
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          123..183
FT                   /note="SH3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          235..296
FT                   /note="SH3 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          184..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         127
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P46109"
FT   MOD_RES         207
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P46109"
FT   CONFLICT        165
FT                   /note="N -> T (in Ref. 1; CAA62220)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   303 AA;  33830 MW;  A8C801F78EF73573 CRC64;
     MSSARFDSSD RSAWYMGPVT RQEAQTRLQG QRHGMFLVRD SSTCPGDYVL SVSENSRVSH
     YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE PAPRYPSPPV GSVSAPNLPT
     AEENLEYVRT LYDFPGNDAE DLPFKKGELL VIIEKPEEQW WSARNKDGRV GMIPVPYVEK
     LVRSSPHGKH GNRNSNSYGI PEPAHAYAQP QTTTPLPTVA STPGAAINPL PSTQNGPVFA
     KAIQKRVPCA YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIFDPQNPD
     DNE
//