ID G1TUV3_RABIT Unreviewed; 764 AA.
AC G1TUV3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=FCH and double SH3 domains 2 {ECO:0000313|Ensembl:ENSOCUP00000020829.3};
GN Name=FCHSD2 {ECO:0000313|Ensembl:ENSOCUP00000020829.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000020829.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000020829.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000020829.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000020829.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000020829.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AAGW02008168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02008169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02008170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02008171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02008172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02008173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02008174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02008175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02008176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02008177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017200323.1; XM_017344834.1.
DR AlphaFoldDB; G1TUV3; -.
DR SMR; G1TUV3; -.
DR STRING; 9986.ENSOCUP00000020829; -.
DR Ensembl; ENSOCUT00000026628.3; ENSOCUP00000020829.3; ENSOCUG00000010457.4.
DR GeneID; 100340980; -.
DR CTD; 9873; -.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00510000046732; -.
DR HOGENOM; CLU_013546_0_0_1; -.
DR InParanoid; G1TUV3; -.
DR OrthoDB; 3674259at2759; -.
DR TreeFam; TF324557; -.
DR Proteomes; UP000001811; Chromosome 1.
DR Bgee; ENSOCUG00000010457; Expressed in aorta and 16 other cell types or tissues.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR GO; GO:0120043; C:stereocilium shaft; IEA:Ensembl.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IEA:Ensembl.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:Ensembl.
DR GO; GO:0061024; P:membrane organization; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IEA:Ensembl.
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 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000001811};
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 657..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 381..415
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 672..693
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 86765 MW; DD7240F9931FC723 CRC64;
MQPPPRKVKV TQELKNIQVE QMTKLQAKHQ AECDLLEDMR TFSQKKAAIE REYAQGMQKL
ASQYLKRDWP GIKADDRNDY RSMYPVWKSF LEGTMQVAQS RINICENYKN FISEPARTVR
SLKEQQLKRC VDQLTKIQTE LQETVKDLAK GKKKYFETEQ MAHAVREKAD IEAKSKLSLF
QSRISLQKAS VKLKARRSEC NSKATHARND YLLTLAAANA HQDRYYQTDL VNIMKALDGN
VYDHLKDYLI AFSRTELETC QAVQNTFQFL LENSNKVVRD YNLQLFLQEN AVFHKPQPFQ
FQPCDSDTSL KAAQLVDIEL SPVSALRMTI AESRQLESET GTTEEHSLNK EARKWATRVA
REHKNIVHQQ RVLNDLEGHG VAVSEQSRVE LEQKIDEARE NIRKAEIIKL KAEARLDLLK
QIGVSVDTWL KSAMSQVMEE LENERWARPP AVTSNGTLHP LNADTEREEG EEFEDNMDAF
DDSSSSPSGT LRNYPLTCKV VYSYKASQPD ELTIEEHEVL EVIEDGDMED WVKARNKVGQ
VGYVPEKYLQ FPTSNSLLSM LQSLAALDSR SHTSSNSTEA ELVSGSLNGD ASVCFVKALY
DYEGQTDDEL SFPEGAIIRI VNKENQDDDG FWEGEFSGRI GVFPSVLVEE LSASENGDTP
WMREIQISPS PKPHTSLPPL PLYDQPPSSP YPSPDKRSSQ YFPRSPSANE NSLHAESPGF
SQASRHTPET SYGKLRPVRA APPPPTQSHR RPAEKIEDVE ITLV
//
