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AF1L1_XENTR
ID   AF1L1_XENTR             Reviewed;         758 AA.
AC   F7EL49;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Actin filament-associated protein 1-like 1;
DE            Short=AFAP1-like protein 1;
GN   Name=afap1l1;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
CC   -!- FUNCTION: May be involved in podosome and invadosome formation.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TED9}. Cell
CC       projection, podosome {ECO:0000250|UniProtKB:Q8TED9}. Cell projection,
CC       invadopodium {ECO:0000250|UniProtKB:Q8TED9}. Cytoplasm, cytoskeleton,
CC       stress fiber {ECO:0000250|UniProtKB:Q8TED9}.
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DR   EMBL; AAMC01088878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F7EL49; -.
DR   SMR; F7EL49; -.
DR   STRING; 8364.ENSXETP00000063750; -.
DR   PaxDb; F7EL49; -.
DR   eggNOG; ENOG502R3HG; Eukaryota.
DR   HOGENOM; CLU_014418_1_0_1; -.
DR   InParanoid; F7EL49; -.
DR   OMA; QCNNTEG; -.
DR   TreeFam; TF332622; -.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR030113; AFAP.
DR   InterPro; IPR030112; AFAP1L1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR14338; PTHR14338; 1.
DR   PANTHER; PTHR14338:SF1; PTHR14338:SF1; 1.
DR   Pfam; PF00169; PH; 2.
DR   SMART; SM00233; PH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   3: Inferred from homology;
KW   Cell junction; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Reference proteome; Repeat.
FT   CHAIN           1..758
FT                   /note="Actin filament-associated protein 1-like 1"
FT                   /id="PRO_0000416694"
FT   DOMAIN          216..312
FT                   /note="PH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          409..503
FT                   /note="PH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          91..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          692..758
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          602..690
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        102..121
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..720
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   758 AA;  85949 MW;  737ABF148768BF7F CRC64;
     MQERLRILDQ LLPELNVLLR LLDHEFLSAT TREKQSAVCS ILRQLQPAPG DELDFQYMNT
     AAYHNGTSFV ESLFEEFDCD LHDLHDMQDE YRDSSENLSC QLPPPPSAPP PPLPTTPPPE
     DYYEEAVPLG PGKFTEYITS RNSSSPPNSI EDGYYEEADN NYPMTRINGE QKNSYNESDG
     LSSSYESYDE EDEEGKAQRL MLQWPSQEAS LHLVRDSRIC AFLLRKKRFG QWAKQLTLIK
     DNKLLCYKSS KDRQPHLEIP LALCNVAYVP KDGRRKKHEL RFSLPNGEML VLAVQSREQA
     EEWLRVIKEV ISPSTGSSPA SPALRHRLDL DKRLSHDKTS DSDSAANGEN SSLSSGKENR
     DTGKCRKGGL AELKGSMSRA AGKKITRIIS FSKKKQSTEE HHTSSTEEEV PCCGYLSVLV
     NQCWKERWCC LKGHTLYFHK DRNDLRTHIN AIALRGCEVS PGFGPLHPFA FRILRQSQEV
     TALEASCSEE MGRWLGLLLA QTGSKTKPEA LHYDYVDVET IANIATAVRH SFLWATSSHS
     STSDLRLYDD VSYEKVEDPK RAPGVAQVKR HASSCSEKSR RVESEVKVKR HASNANQYKY
     GKTRAEEDAR KFIVEKEKLE KEKEAIRSKL IAMKRERREL KEMLKNCSGK QQKEMEERLA
     MLEEQCKNNE KVRVDLEIQL TEVKENLKKS LAGGPTLGLA VTGKSENPPQ KSQQPRSPPD
     RLLPVNSAAE MRRRSPSIAA SSKGKVLQKA KEWEKKKP
 
 
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