ID A0A0G2K219_RAT Unreviewed; 764 AA.
AC A0A0G2K219;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=FCH and double SH3 domains 2 {ECO:0000313|Ensembl:ENSRNOP00000072072.2};
GN Name=Fchsd2 {ECO:0000313|Ensembl:ENSRNOP00000072072.2,
GN ECO:0000313|RGD:1304812};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000072072.2, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000072072.2, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000072072.2,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000072072.2}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000072072.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 10116.ENSRNOP00000072072; -.
DR Ensembl; ENSRNOT00000091822.2; ENSRNOP00000072072.2; ENSRNOG00000019319.8.
DR AGR; RGD:1304812; -.
DR RGD; 1304812; Fchsd2.
DR VEuPathDB; HostDB:ENSRNOG00000019319; -.
DR GeneTree; ENSGT00510000046732; -.
DR InParanoid; A0A0G2K219; -.
DR OMA; TPMMEEP; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019319; Expressed in spleen and 19 other cell types or tissues.
DR ExpressionAtlas; A0A0G2K219; baseline and differential.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0120043; C:stereocilium shaft; ISO:RGD.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:RGD.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:RGD.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISO:RGD.
DR GO; GO:0061024; P:membrane organization; ISO:RGD.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; ISO:RGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR CDD; cd07677; F-BAR_FCHSD2; 1.
DR CDD; cd11894; SH3_FCHSD2_2; 1.
DR CDD; cd11761; SH3_FCHSD_1; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR034934; FCHSD2_F-BAR_dom.
DR InterPro; IPR035556; FCHSD2_SH3_2.
DR InterPro; IPR035460; FCHSD_SH3_1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15735:SF11; F-BAR AND DOUBLE SH3 DOMAINS PROTEIN 2; 1.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2K219};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 8..282
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 493..554
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 591..653
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 653..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 381..415
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 655..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..693
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 86794 MW; 7560BA4CEC9BE371 CRC64;
MQPPPRKVKV TQELRNIQGE QMTKLQAKHQ AECDLLEDMR TFSQKKAAIE REYAQGIQKL
ASQYLKRDWP GIKTDDRNDY RSMYPVWKSF LEATMQVAQS RINICENYKN FISEPARAVR
SLKEQQLKRC VDQLTKIQTE LQETVKDLVK GKKKYFETEQ MAHAVREKAD IEAKSKLSLF
QSRISLQKAS VKLKARRTEC NTKATHARND YLLTLAAANA HQDRYYQTDL LNIMKALDGN
VYDHLKDYLI AFSRTELEAC QAMQNTFQFL LENSSKVVRD YNLQLFLQEN AVFHKPQPFQ
FQPCDSDTSL KAAQLVDIEL SPVSALRMTI AESRQLESET GTTEEHSLNK EARKWATRVA
REHKNIVHQQ RVLNELECHG VAVSEQSRAE LEQKIDEARE NIRKAEIIKL KAEARLDLLK
QIGVSVDTWL KSAMNQVMEE LENERWARPP AVTSNGTLHS LNADAEREEG EEFEDNMDVF
DDSSSSPSGT LRNYPLTCKV VYSYKASQPD ELTIEEHEVL EVIEDGDMED WVKARNKVGQ
VGYVPEKYLQ FPTSNSLLSM LQSLAALDSR SHTSSNSTEA ELVSGSLNGD ASVCFVKALY
DYEGQTDDEL SFPEGAIIRI VNKENQDDDG FWEGEFSGRI GVFPSVLVEE LSASENGDTP
WTRDIQVSPS PKPHTSLPPL PLYDQPPSSP YPSPDKRSSQ FFPRSPSANE NCLHAESPGF
SQASRQTPDT SYGKLRPVRA APPPPTQTHR RTAEKMEDVE ITLV
//
