ID   AF1L2_XENLA             Reviewed;         811 AA.
AC   Q6PF55;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Actin filament-associated protein 1-like 2;
DE            Short=AFAP1-like protein 2;
GN   Name=afap1l2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in a signaling cascade by enhancing the
CC       kinase activity of src. Contributes to src-regulated transcription
CC       activation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with src. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; BC057722; AAH57722.1; -; mRNA.
DR   RefSeq; NP_001079952.1; NM_001086483.1.
DR   AlphaFoldDB; Q6PF55; -.
DR   SMR; Q6PF55; -.
DR   DNASU; 379643; -.
DR   GeneID; 379643; -.
DR   KEGG; xla:379643; -.
DR   CTD; 379643; -.
DR   Xenbase; XB-GENE-6255187; afap1l2.L.
DR   OrthoDB; 256810at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 379643; Expressed in internal ear and 15 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035591; F:signaling adaptor activity; IEA:InterPro.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR030113; AFAP.
DR   InterPro; IPR030115; AFAP1L2.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR14338; PTHR14338; 1.
DR   PANTHER; PTHR14338:SF4; PTHR14338:SF4; 1.
DR   Pfam; PF00169; PH; 2.
DR   SMART; SM00233; PH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Reference proteome; Repeat.
FT   CHAIN           1..811
FT                   /note="Actin filament-associated protein 1-like 2"
FT                   /id="PRO_0000361277"
FT   DOMAIN          181..277
FT                   /note="PH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          359..453
FT                   /note="PH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          67..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          642..737
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        517..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..581
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   811 AA;  90908 MW;  1CBAE773A77DA7A0 CRC64;
     MERYKGLERL LSELEEFLFI LDKENLSSAA VLKKSIVSEI LQLFIKSNSS CDEEYIYMNK
     VLETDKKEAQ GKQGKAQVLD PPAKETLTNG TAGQHLAPPQ KSLPDLPPPK IITEKLPVSK
     CDSPEGYYEE AEPYNASFND DGEAVSSSYE SYDEDESNKS KSAMQQHQWP STEASIELMK
     DAMICAFLWR KKWLGQWAKQ LCVVKDTRLM CYKTSKDHNP QLDVNLIGCS VSYKEKQVRR
     KEHKLKITPT NTDVIVLGMQ SKEQAEQWLK VIQDISGLQS DPLCDSSVIT ADGQRQIHPK
     AEGTDRHSGA SESGSSTDGH PETPEIKEVK KKVTSGLKLS NLMNLGRKKS TSMESPDKAL
     ETSNYLNVLI NSQWKSRYCC IKDGQLHFYQ DRNKTKNAAQ PVSLIGCDII PQPTQDHLYS
     FRILQNGEEL ATLEAKSSED MGHWLGLLLL ESGSRSDPED FTYDYVDADR VSCIVSAAKN
     SYFLMQRKYC EPNTYIDAPR GQRYQQDDLY DDVDMSDIQG DEPKSEEKGE AEDKMYLDLI
     PTRSFLHSVG IKSLCQALGS PGPERVSGKK DNEESERGTL SCREQDSSGQ VTEETKQVTE
     DPPQQTSPGT PIIGPSVSAS PRLEKSNKER VKATNHVAIE TLLGKNRTEA EIKRFTEEKE
     KLEKEREEIR VQLAQLRKER REMKETVTNC PDKGLLTDLE DKLRLKEEQC KERESYRVDL
     ELKLVEVKEN LRKAELGPAT LGTSVEPAHL DTTAPSIKSC SPTHAPECSP VTATVGSPVN
     SAVALKSRPQ PIVTTGKVLQ KAKEWEKKGA S