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CD2-associated protein

 CD2AP_RAT               Reviewed;         637 AA.
F1LRS8; Q7TSS5;
22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
22-JAN-2014, sequence version 2.
22-NOV-2017, entry version 55.
RecName: Full=CD2-associated protein;
Name=Cd2ap;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Kawachi H., Koike H., Shimizu F.;
"Rat CD2AP.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
FUNCTION IN RET STABILITY, INTERACTION WITH CBLC AND RET, AND TISSUE
SPECIFICITY.
PubMed=18753381; DOI=10.1523/JNEUROSCI.2738-08.2008;
Tsui C.C., Pierchala B.A.;
"CD2AP and Cbl-3/Cbl-c constitute a critical checkpoint in the
regulation of ret signal transduction.";
J. Neurosci. 28:8789-8800(2008).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458; SER-469; SER-510
AND SER-514, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Seems to act as an adapter protein between membrane
proteins and the actin cytoskeleton (By similarity). In
collaboration with CBLC, modulates the rate of RET turnover and
may act as regulatory checkpoint that limits the potency of GDNF
on neuronal survival. Controls CBLC function, converting it from
an inhibitor to a promoter of RET degradation (PubMed:18753381).
May play a role in receptor clustering and cytoskeletal polarity
in the junction between T-cell and antigen-presenting cell (By
similarity). May anchor the podocyte slit diaphragm to the actin
cytoskeleton in renal glomerolus. Also required for cytokinesis.
Plays a role in epithelial cell junctions formation (By
similarity). {ECO:0000250|UniProtKB:Q9JLQ0,
ECO:0000250|UniProtKB:Q9Y5K6, ECO:0000269|PubMed:18753381}.
-!- SUBUNIT: Homodimer. Interacts with F-actin, PKD2, NPHS1 and NPHS2.
Interacts with WTIP. Interacts with DDN; interaction is direct.
Interacts (via SH3 2 domain) with CBL (via phosphorylated C-
terminus). Interacts with BCAR1/p130Cas (via SH3 domain).
Interacts with MVB12A and ARHGAP17. Interacts with ANLN, CD2 and
CBLB. Interacts with PDCD6IP and TSG101. Interacts with RIN3.
Interacts directly with RET (inactive) and CBLC; upon RET
activation by GDNF suggested to dissociate from RET as CBLC:CD2AP
complex. Interacts with CGNL1 and SH3BP1; probably part of a
complex at cell junctions. Interacts with CAPZA1.
{ECO:0000250|UniProtKB:Q9Y5K6, ECO:0000269|PubMed:18753381,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q9Y5K6}. Cell projection, ruffle
{ECO:0000250|UniProtKB:Q9Y5K6}. Cell junction
{ECO:0000250|UniProtKB:Q9Y5K6}. Note=Colocalizes with F-actin and
BCAR1/p130Cas in membrane ruffles (By similarity). Located at
podocyte slit diaphragm between podocyte foot processes (By
similarity). During late anaphase and telophase, concentrates in
the vicinity of the midzone microtubules and in the midbody in
late telophase (By similarity). {ECO:0000250|UniProtKB:Q9JLQ0,
ECO:0000250|UniProtKB:Q9Y5K6}.
-!- TISSUE SPECIFICITY: Expressed in neurons and renal glomerular
podocytes (at protein level). {ECO:0000269|PubMed:18753381}.
-!- DOMAIN: The Pro-rich domain may mediate binding to SH3 domains.
{ECO:0000250}.
-!- DOMAIN: Potential homodimerization is mediated by the coiled coil
domain. {ECO:0000250}.
-!- PTM: Phosphorylated on tyrosine residues; probably by c-Abl, Fyn
and c-Src. {ECO:0000250}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY114147; AAM47029.1; -; mRNA.
EMBL; AABR06058949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06058950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06058951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
UniGene; Rn.212220; -.
UniGene; Rn.33933; -.
SMR; F1LRS8; -.
CORUM; F1LRS8; -.
STRING; 10116.ENSRNOP00000016291; -.
iPTMnet; F1LRS8; -.
PhosphoSitePlus; F1LRS8; -.
PaxDb; F1LRS8; -.
PRIDE; F1LRS8; -.
Ensembl; ENSRNOT00000016291; ENSRNOP00000016291; ENSRNOG00000011987.
RGD; 727803; Cd2ap.
eggNOG; KOG4348; Eukaryota.
eggNOG; ENOG410XQBY; LUCA.
GeneTree; ENSGT00530000063594; -.
HOGENOM; HOG000231405; -.
HOVERGEN; HBG057824; -.
InParanoid; F1LRS8; -.
OMA; YDAVHDD; -.
OrthoDB; EOG091G041Q; -.
TreeFam; TF350191; -.
PRO; PR:F1LRS8; -.
Proteomes; UP000002494; Chromosome 9.
Bgee; ENSRNOG00000011987; -.
GO; GO:0031252; C:cell leading edge; IDA:RGD.
GO; GO:0005911; C:cell-cell junction; ISO:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0030139; C:endocytic vesicle; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0031941; C:filamentous actin; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0001726; C:ruffle; ISO:RGD.
GO; GO:0008013; F:beta-catenin binding; IDA:RGD.
GO; GO:0045296; F:cadherin binding; IPI:RGD.
GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
GO; GO:0005172; F:vascular endothelial growth factor receptor binding; IDA:RGD.
GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IMP:RGD.
GO; GO:0098609; P:cell-cell adhesion; IMP:RGD.
GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; ISS:UniProtKB.
GO; GO:0032911; P:negative regulation of transforming growth factor beta1 production; ISO:RGD.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:RGD.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:RGD.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISO:RGD.
GO; GO:0048259; P:regulation of receptor-mediated endocytosis; IDA:RGD.
GO; GO:0016050; P:vesicle organization; IDA:RGD.
CDD; cd12053; SH3_CD2AP_1; 1.
CDD; cd12054; SH3_CD2AP_2; 1.
CDD; cd12056; SH3_CD2AP_3; 1.
InterPro; IPR028445; CD2AP.
InterPro; IPR035775; CD2AP_SH3_1.
InterPro; IPR035777; CD2AP_SH3_3.
InterPro; IPR035776; CD2AP_SH_2.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR14167:SF23; PTHR14167:SF23; 1.
Pfam; PF00018; SH3_1; 1.
Pfam; PF14604; SH3_9; 2.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 3.
SUPFAM; SSF50044; SSF50044; 3.
PROSITE; PS50002; SH3; 3.
1: Evidence at protein level;
Cell cycle; Cell division; Cell junction; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Isopeptide bond; Mitosis; Phosphoprotein; Reference proteome; Repeat;
SH3 domain; SH3-binding; Ubl conjugation.
CHAIN 1 637 CD2-associated protein.
/FTId=PRO_0000424877.
DOMAIN 1 59 SH3 1; truncated. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 108 167 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 269 330 SH3 3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 1 175 Interaction with ANLN and localization to
the midbody. {ECO:0000250}.
COILED 580 635 {ECO:0000255}.
MOTIF 336 352 SH3-binding. {ECO:0000255}.
MOTIF 378 397 SH3-binding. {ECO:0000255}.
MOTIF 410 422 SH3-binding. {ECO:0000255}.
COMPBIAS 336 422 Pro-rich.
MOD_RES 80 80 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y5K6}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y5K6}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y5K6}.
MOD_RES 458 458 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 510 510 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 514 514 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 580 580 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y5K6}.
CROSSLNK 58 58 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9Y5K6}.
CROSSLNK 523 523 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9Y5K6}.
CONFLICT 169 169 D -> E (in Ref. 1; AAM47029).
{ECO:0000305}.
CONFLICT 185 185 T -> S (in Ref. 1; AAM47029).
{ECO:0000305}.
CONFLICT 450 450 E -> D (in Ref. 1; AAM47029).
{ECO:0000305}.
SEQUENCE 637 AA; 70491 MW; 772F9EDFF65BA19B CRC64;
MVDYIVEYDY DAVHDDELTI RVGEIIRNVK KLQEEGWLEG ELNGRRGMFP DNFVKEIKRE
TEPKDDNLPI KRERPGNVAS LVQRISTYGL PAGGIQPHPQ TKAMKKKTKK RQCKVLFEYS
PQNEDELELT VGDVIDVIEE VEEGWWSGTL NNKLGLFPSN FVKELESTDD GEMHDAQEES
EVSLTGPTSP MPSPGNGSEP APGSVTQPKK IRGVGFGDIF KEGSVKLRTR TSSSETEEKK
SEKPLILQSL GSRTQNVEVT KPDIDGKIKA KEYCKTVFPY TGTNEDELTF REGEIIHLIS
KETGEAGWWK GELNGKEGVF PDNFAVQISE LDKDFPKPKK PPPPAKGPAP KPDPLAGEKK
TFPLKAEDRD EKSLLEQKPS KPAAPQVPPK KPTPPTKANN LLRSPGTMYP KRPEKPVPPP
PPTAKINGEV STISSKIDTE PLSKPKLDPE QLPVRPKSVD LDALVARNSK ETDNVNFDDI
ASSENLLHLT ANRPKMPGRR LPGRFNGGHS PTQSPEKTLK LPKDDDSGNI KPSEFKKDAG
YSSKPSLSAP SSASKVNTAA FLSPLELKAK VEADDGKKSS LDELRAQIIE LLCIVDALKK
DHGKELEKLR RELEEEKAMR SNLEVEIAKL KKAVLLS


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