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Database: UniProt
Entry: Q6GL36_XENTR
LinkDB: Q6GL36_XENTR
Original site: Q6GL36_XENTR 
ID   Q6GL36_XENTR            Unreviewed;       876 AA.
AC   Q6GL36;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=Villin 1 {ECO:0000313|EMBL:AAH74679.1};
DE   SubName: Full=Villin-like protein {ECO:0000313|RefSeq:NP_001005657.1};
GN   Name=vill {ECO:0000313|RefSeq:NP_001005657.1,
GN   ECO:0000313|Xenbase:XB-GENE-945607};
GN   Synonyms=vil1 {ECO:0000313|EMBL:AAH74679.1,
GN   ECO:0000313|RefSeq:NP_001005657.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|EMBL:AAH74679.1};
RN   [1] {ECO:0000313|RefSeq:NP_001005657.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH74679.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAH74679.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001005657.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the villin/gelsolin family.
CC       {ECO:0000256|ARBA:ARBA00008418}.
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DR   EMBL; BC074679; AAH74679.1; -; mRNA.
DR   RefSeq; NP_001005657.1; NM_001005657.1.
DR   GeneID; 448145; -.
DR   KEGG; xtr:448145; -.
DR   AGR; Xenbase:XB-GENE-945607; -.
DR   CTD; 50853; -.
DR   Xenbase; XB-GENE-945607; vill.
DR   OMA; TINKMRM; -.
DR   OrthoDB; 25995at2759; -.
DR   Proteomes; UP000008143; Chromosome 6.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   CDD; cd11290; gelsolin_S1_like; 1.
DR   CDD; cd11289; gelsolin_S2_like; 1.
DR   CDD; cd11292; gelsolin_S3_like; 1.
DR   CDD; cd11293; gelsolin_S4_like; 1.
DR   CDD; cd11288; gelsolin_S5_like; 1.
DR   CDD; cd11291; gelsolin_S6_like; 1.
DR   Gene3D; 3.40.20.10; Severin; 6.
DR   Gene3D; 1.10.950.10; Villin headpiece domain; 1.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR007123; Gelsolin-like_dom.
DR   InterPro; IPR036180; Gelsolin-like_dom_sf.
DR   InterPro; IPR007122; Villin/Gelsolin.
DR   InterPro; IPR003128; Villin_headpiece.
DR   InterPro; IPR036886; Villin_headpiece_dom_sf.
DR   PANTHER; PTHR11977; VILLIN; 1.
DR   PANTHER; PTHR11977:SF30; VILLIN-LIKE PROTEIN; 1.
DR   Pfam; PF00626; Gelsolin; 6.
DR   Pfam; PF02209; VHP; 1.
DR   PRINTS; PR00597; GELSOLIN.
DR   SMART; SM00262; GEL; 6.
DR   SMART; SM00153; VHP; 1.
DR   SUPFAM; SSF55753; Actin depolymerizing proteins; 4.
DR   SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 2.
DR   SUPFAM; SSF47050; VHP, Villin headpiece domain; 1.
DR   PROSITE; PS51089; HP; 1.
PE   2: Evidence at transcript level;
KW   Actin capping {ECO:0000256|ARBA:ARBA00022467};
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008143}.
FT   DOMAIN          810..876
FT                   /note="HP"
FT                   /evidence="ECO:0000259|PROSITE:PS51089"
FT   REGION          744..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          784..814
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   876 AA;  98599 MW;  4BBFA088E846668C CRC64;
     MTQNLENMCR KPGLQIWSME KMKLVPIPEK AYGSFFEGDC YILLYNKQTP NGLISDIHYW
     IGKDSSQDEQ GSAAFYATQI DGLLGGGPIQ HREVQGHESA TFKSYFKNGV IYKKGGVSSG
     FKHVETNMYN IRRLLHVKGK KHVTATEVAM SWNSFNKGDV FLLDLGKVII QWNGPESNKS
     ERIRACSLAQ SIRDDERGGR AQIGVIDNEQ DSPDLMQIMV AVLGARTGEL KDSVPDEKAD
     EQQKANVRLY HVFEKDANLV VQELATKPLT QDLLQHEDCH ILDQGGVKIY VWRGKNSSPE
     EKSAAFSRAV GFIQAKGYPP TTNVEVVNDG AESAMFKQLF QNWKDVGETQ GLGKTFSVGK
     IAKVEQTKFD VNQLYARPEL AAEQRMVDDA SGNVEVWRIE KLELAEVEPR TYGQFYGGDC
     YLILYTYMKS GRPNYLLYMW LGRHASQDEI TACAFQAVQL DKKYHDQPVQ IRVTMGKEPR
     HLQAMFKGKM IIYEGGTSRL GVHEPEAPIK LFQVKGTNEY NTKATEVPAR ASSLNSNDVF
     VLKTESMCYL WCGKGCSGDE REMAKTVANI ISKQDKQTIL EGQEPAEFWV ALGGKAPYAS
     DKRFQEQAVQ YSPRLFECSN QTGRFVMTEV VDFCQSDLDE DDVMLLDTWE EIFLWVGKSA
     NDYEKTESVK ASQEYLRAHP AGRDLATPII LVKQGHEPPT FTGWFNAWDS HKWSSDLSYE
     DMKKTLGDVS AISQISVDLQ NTNLNKKSTS NAPPTSSAPP TSSAPESVPI PMYRSHSQEN
     LQYNNGHQAT TNGSQVPNQV KQNPEPLPES NGNQWFDRSF LINKVTEDLP DGVDPTKKEM
     YLSDADFAAI MGMPKAQFYQ MPKWKQQNLK KQHGLF
//
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