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AF1L1_RAT
ID   AF1L1_RAT               Reviewed;         767 AA.
AC   D4AB98;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Actin filament-associated protein 1-like 1;
DE            Short=AFAP1-like protein 1;
GN   Name=Afap1l1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-93; SER-97 AND
RP   SER-103, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: May be involved in podosome and invadosome formation.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CTTN. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection,
CC       podosome {ECO:0000250}. Cell projection, invadopodium {ECO:0000250}.
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DR   EMBL; CH473971; EDM14621.1; -; Genomic_DNA.
DR   RefSeq; NP_001099612.1; NM_001106142.1.
DR   AlphaFoldDB; D4AB98; -.
DR   STRING; 10116.ENSRNOP00000026495; -.
DR   iPTMnet; D4AB98; -.
DR   PhosphoSitePlus; D4AB98; -.
DR   jPOST; D4AB98; -.
DR   PaxDb; D4AB98; -.
DR   PRIDE; D4AB98; -.
DR   GeneID; 291565; -.
DR   KEGG; rno:291565; -.
DR   CTD; 134265; -.
DR   RGD; 1311580; Afap1l1.
DR   VEuPathDB; HostDB:ENSRNOG00000019403; -.
DR   eggNOG; ENOG502R3HG; Eukaryota.
DR   HOGENOM; CLU_014418_1_0_1; -.
DR   InParanoid; D4AB98; -.
DR   OMA; QCNNTEG; -.
DR   OrthoDB; 256810at2759; -.
DR   PRO; PR:D4AB98; -.
DR   Proteomes; UP000002494; Chromosome 18.
DR   Proteomes; UP000234681; Chromosome 18.
DR   Bgee; ENSRNOG00000019403; Expressed in skeletal muscle tissue and 18 other tissues.
DR   Genevisible; D4AB98; RN.
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   1: Evidence at protein level;
KW   Cell junction; Cell projection; Coiled coil; Cytoplasm; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..767
FT                   /note="Actin filament-associated protein 1-like 1"
FT                   /id="PRO_0000416693"
FT   DOMAIN          219..315
FT                   /note="PH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          417..511
FT                   /note="PH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          83..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          704..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          610..700
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        83..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..124
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..597
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..733
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         97
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         103
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BZI0"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BZI0"
FT   MOD_RES         342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BZI0"
FT   MOD_RES         556
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BZI0"
FT   MOD_RES         746
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BZI0"
SQ   SEQUENCE   767 AA;  86875 MW;  15E1C7A5707AEB58 CRC64;
     MDRSRVLEQL IPELTRLLSL LDHEYLSDST LEKKMAVASL LQSLQPLPAK EVSFLYVNTA
     DLHSGPSFVE SLFEEFDCDL GDLRDMSDDG ERSKEASPEP IKSPSLRSTA DVPPPLPNKP
     PPEDYYEEAL PLGPGKSPEY ISSHNGCSPA QSIVDGYYED ADSSYPTTRM NGESKSSYND
     SDAMSSSYES YDEEEEEEKG RQPKHQWPSE EASMHLVRDC RICAFLLRKK RFGQWAKQLT
     VIKEEQLLCY KSSKDRQPHL RLPLDVCTVV YVPKDSRHKR HELRFSQGAT EVLVLALQSR
     EQAEEWLKVI REVSRPIGGA ESLEVPRSPV ILCKLDQDKR LSQEKQNSDS DSLGMNDSSS
     TLSRREACEH GKGKKNSLAE LKDSMSRAAG RKITRIISFS KKKALSEDLQ TFSSEDEAPC
     CGYLNVLVNH GWKERWCRLR CNTLYFHKDR TDLHTHVNAI ALRGCEVAPG FGPRHPFAFR
     ILRNRQEVAI LEASCSEDMG RWLGLLLVEM GSKVTPEALH YDYVDVETLT SIVSAGRNSF
     LYAQSCQDQW PEPRIYDEVP YEKVQDEEPQ RPTGAQVKRH ASSCSEKSHR ADPQVKVKRH
     ASSANQYKYG KNRAEEDARR YLVEKERLEK EKETIRTELT ALRQEKKELK EAIRNNPGAK
     LKALEEAVAT LDAQCRAKEE QRIDLELKLV AVKERLQQSL AGGPALGLSV SSKSKSQETT
     NKPQSSVPEQ SLPVNCVSEM RKRSPSIVTS NQGRVLQKAK EWEMKKT
 
 
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