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Database: UniProt
Entry: K7FEV4_PELSI
LinkDB: K7FEV4_PELSI
Original site: K7FEV4_PELSI 
ID   K7FEV4_PELSI            Unreviewed;       617 AA.
AC   K7FEV4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Formin binding protein 1 {ECO:0000313|Ensembl:ENSPSIP00000006564.1};
GN   Name=FNBP1 {ECO:0000313|Ensembl:ENSPSIP00000006564.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000006564.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000006564.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000256|ARBA:ARBA00004544}.
CC   -!- SIMILARITY: Belongs to the FNBP1 family.
CC       {ECO:0000256|ARBA:ARBA00009426}.
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DR   EMBL; AGCU01121699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01121700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01121701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01121702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01121703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01121704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01121705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01121706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01121707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01121708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006128407.1; XM_006128345.2.
DR   AlphaFoldDB; K7FEV4; -.
DR   STRING; 13735.ENSPSIP00000006564; -.
DR   Ensembl; ENSPSIT00000006601.1; ENSPSIP00000006564.1; ENSPSIG00000005955.1.
DR   GeneID; 102451364; -.
DR   KEGG; pss:102451364; -.
DR   CTD; 23048; -.
DR   eggNOG; KOG3565; Eukaryota.
DR   GeneTree; ENSGT00950000183047; -.
DR   HOGENOM; CLU_023320_2_0_1; -.
DR   OMA; XQNEGTI; -.
DR   OrthoDB; 2995634at2759; -.
DR   TreeFam; TF351162; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd07676; F-BAR_FBP17; 1.
DR   CDD; cd11629; HR1_FBP17; 1.
DR   Gene3D; 6.10.140.470; -; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR037449; FNBP1_F-BAR.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR   PANTHER; PTHR15735:SF13; FORMIN-BINDING PROTEIN 1; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS51860; REM_1; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..264
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          404..481
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          550..611
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          294..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          490..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          411..438
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        336..351
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   617 AA;  71393 MW;  EA5673A06A0E01A3 CRC64;
     MSWGTELWDQ FDNLEKHTQW GIDVLEKYIK FVKERTEIEI SYAKQLRNLS KKYQPKKNSK
     EEEEYKYTSC KAFLVTLNEM NDYAGQHEVI SENMTSQITA ELTRYMQELK QERKSYFHDG
     RKAQQYIETC WKQLEASKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQIRH
     QMAEDSKAEY SSSLQKFNHE QHEHYHTHIP NIFQKIQEME ERRIVRIGEC MKTYAEVDRQ
     VIPIIGKCLD GITKAAESID QKNDSQLVIE AFKSGFEPPG DIDFEDFTQP MKRTVSETSL
     SNSRGDGKSE PKFGGKSKGK LWPFIKKNKL MSLLTSPHQP PPPPPASASP SAVPNGPQSP
     KQQKEPLSHR FNEFMTSKPK IHCFRSLKRG LSLKLGGGPE DFSNLPPEQR RKKLQQKVDE
     LNKDIQKEMD QRDALTKMKD VYIKNPQMGD AASVDYKLAE LGQNMEKLRL EAQKFEGWLA
     EVEGRLPVRT EQSRRQSGMY ETQNTSAVNN CAQDRESPDG SYTEEQSQES EMKVPMTEFD
     DEFDDEEPLP TIGTCKALYT FEGQNEGTIS VAEGELLYVI EEDKGDGWTR IRRNENEEGY
     VPTSYVEVYL DKNAKDS
//
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