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Database: UniProt
Entry: G1LT49_AILME
LinkDB: G1LT49_AILME
Original site: G1LT49_AILME 
ID   G1LT49_AILME            Unreviewed;       605 AA.
AC   G1LT49;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Formin-binding protein 1-like {ECO:0000256|ARBA:ARBA00019975};
DE   AltName: Full=Transducer of Cdc42-dependent actin assembly protein 1 {ECO:0000256|ARBA:ARBA00032854};
GN   Name=FNBP1L {ECO:0000313|Ensembl:ENSAMEP00000010245.2};
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000010245.2, ECO:0000313|Proteomes:UP000008912};
RN   [1] {ECO:0000313|Ensembl:ENSAMEP00000010245.2, ECO:0000313|Proteomes:UP000008912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
RN   [2] {ECO:0000313|Ensembl:ENSAMEP00000010245.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}. Cytoplasmic vesicle
CC       {ECO:0000256|ARBA:ARBA00004541}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}. Vesicle
CC       {ECO:0000256|ARBA:ARBA00004373}.
CC   -!- SIMILARITY: Belongs to the FNBP1 family.
CC       {ECO:0000256|ARBA:ARBA00009426}.
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DR   AlphaFoldDB; G1LT49; -.
DR   Ensembl; ENSAMET00000010693.2; ENSAMEP00000010245.2; ENSAMEG00000009719.2.
DR   GeneTree; ENSGT00950000183047; -.
DR   InParanoid; G1LT49; -.
DR   Proteomes; UP000008912; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051020; F:GTPase binding; IEA:Ensembl.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:Ensembl.
DR   GO; GO:0010324; P:membrane invagination; IEA:Ensembl.
DR   GO; GO:0097320; P:plasma membrane tubulation; IEA:Ensembl.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0006900; P:vesicle budding from membrane; IEA:Ensembl.
DR   GO; GO:0030050; P:vesicle transport along actin filament; IEA:Ensembl.
DR   CDD; cd07675; F-BAR_FNBP1L; 1.
DR   CDD; cd11628; HR1_CIP4_FNBP1L; 1.
DR   CDD; cd12072; SH3_FNBP1L; 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; IPR035494; FNBP1L_F-BAR.
DR   InterPro; IPR035493; FNBP1L_SH3.
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:SF14; FORMIN-BINDING PROTEIN 1-LIKE; 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   Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW   ProRule:PRU01077}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
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:UP000008912};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..263
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          397..474
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          538..599
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          325..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          130..174
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          404..438
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        476..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   605 AA;  70136 MW;  0B9F19FE1E2BBE42 CRC64;
     MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSSK
     DEEPRFTSCI AFFNILNELN DYAGQREVVA EEMAHRVYGE LMRYAHDLKT ERKMHLQEGR
     KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH
     MADENKNEYA AQLQNFNGEQ HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV
     IPIISKCLEG MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS
     ASKQESGKMD SKTTVGKPKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS QFLTFSIEPV
     HYCMNEIKTG KPRIPSFRSL KRGWSVKMGP ALEDFSHLPP EQRRKKLQQR IDELNRELQK
     ESDQKEALNK MKDVYEKNPQ MGDPGSLQPK LAETMNNIDR LRMEIHKNEA WLSEVEGKTG
     GRGDRRHSSD INHLVTQGRE SPEGSYTDDA NQEVRGPPQQ HGHHNEFDDE FEDDDPLPAI
     GHCKAIYPFD GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TSYIDVTLEK
     NSKGS
//
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