AF1L1_MOUSE
ID AF1L1_MOUSE Reviewed; 768 AA.
AC Q8BZI0; Q8BKB8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Actin filament-associated protein 1-like 1;
DE Short=AFAP1-like protein 1;
GN Name=Afap1l1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-329; TYR-557 AND
RP SER-747, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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|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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BZI0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BZI0-2; Sequence=VSP_026860, VSP_026861;
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DR EMBL; AK035227; BAC28988.1; -; mRNA.
DR EMBL; AK053714; BAC35486.1; -; mRNA.
DR CCDS; CCDS50303.1; -. [Q8BZI0-1]
DR RefSeq; NP_849259.2; NM_178928.4. [Q8BZI0-1]
DR AlphaFoldDB; Q8BZI0; -.
DR STRING; 10090.ENSMUSP00000113286; -.
DR iPTMnet; Q8BZI0; -.
DR PhosphoSitePlus; Q8BZI0; -.
DR jPOST; Q8BZI0; -.
DR MaxQB; Q8BZI0; -.
DR PaxDb; Q8BZI0; -.
DR PRIDE; Q8BZI0; -.
DR ProteomicsDB; 285556; -. [Q8BZI0-1]
DR ProteomicsDB; 285557; -. [Q8BZI0-2]
DR Antibodypedia; 2023; 73 antibodies from 20 providers.
DR DNASU; 106877; -.
DR Ensembl; ENSMUST00000120472; ENSMUSP00000113286; ENSMUSG00000033032. [Q8BZI0-1]
DR GeneID; 106877; -.
DR KEGG; mmu:106877; -.
DR UCSC; uc008fcq.1; mouse. [Q8BZI0-1]
DR CTD; 134265; -.
DR MGI; MGI:2147199; Afap1l1.
DR VEuPathDB; HostDB:ENSMUSG00000033032; -.
DR eggNOG; ENOG502R3HG; Eukaryota.
DR GeneTree; ENSGT00950000183067; -.
DR HOGENOM; CLU_014418_1_0_1; -.
DR InParanoid; Q8BZI0; -.
DR OMA; QCNNTEG; -.
DR PhylomeDB; Q8BZI0; -.
DR TreeFam; TF332622; -.
DR BioGRID-ORCS; 106877; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Afap1l1; mouse.
DR PRO; PR:Q8BZI0; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8BZI0; protein.
DR Bgee; ENSMUSG00000033032; Expressed in interventricular septum and 210 other tissues.
DR ExpressionAtlas; Q8BZI0; baseline and differential.
DR Genevisible; Q8BZI0; MM.
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 Alternative splicing; Cell junction; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..768
FT /note="Actin filament-associated protein 1-like 1"
FT /id="PRO_0000295240"
FT DOMAIN 220..316
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 418..512
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 165..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 611..701
FT /evidence="ECO:0000255"
FT COMPBIAS 165..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4AB98"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4AB98"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4AB98"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4AB98"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 557
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 373..458
FT /note="KGKKNSLAELKGSMSRAAGRKITRIISFSKKKALSEDLQTFSSEDEVPCCGY
FT LNVLVNQGWKERWCRLRCNTLYFHKDRTDLHTHV -> RSYHELPLVHAGECQRWEGLC
FT YRSTVTEQITGTRVRPLGLSYLVITGRLQGLLGRPEVGRSGTVASFPIPVSPLLWCQAK
FT GRRTAWLSLRAP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026860"
FT VAR_SEQ 459..768
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026861"
SQ SEQUENCE 768 AA; 86638 MW; 5913993426EBCFB2 CRC64;
MDRSRVLEQL IPELTGLLSL LDHEYLSDST LEKKMAVASL LQSLQPLPAK EVSFLYVNTA
DLHSGPSFVE SLFEEFDCDL GDLRDMSDDG EPSKGASPEP TKSPSLRSAA ADVPPPLPNK
PPPEDYYEEA LPLGPGKSPE YISSHNGCSP AQSIVDGYYE DADNSYPTTR MNGELKNSYN
DSDAMSSSYE SYDEEEEEEK GRQPKHQWPS EEASMHLVRD CRICAFLLRK KRFGQWAKQL
TVIKEEQLLC YKSSKDRQPH LRLALDVCTV IYVPKDSRHK RHELRFSQGA TEVLVLALQS
REQAEEWLKV IREVSRPIVG AEGLEVPRSP VILCKADQDK RLSQEKQNSD SDSLGMNDSG
STLGRREACE HGKGKKNSLA ELKGSMSRAA GRKITRIISF SKKKALSEDL QTFSSEDEVP
CCGYLNVLVN QGWKERWCRL RCNTLYFHKD RTDLHTHVNS IALRGCEVAP GFGPRHPFAF
RILRNRQEVA ILEASCSEDM GRWLGLLLVE MGSKVTPEAL HYDYVDVETL TSIVSAGRNS
FLYAQSCQDQ WPEPRIYDEV PYEKVQDEEP QRPTGAQVKR HASSCSEKSH RADPQVKVKR
HASSANQYKY GKNRAEEDAR RYLVEKERLE KEKETIRTEL TALRQEKKEL KEAIRNNPGA
KSKALEEAVA TLEAQCRAKE EQRIDLELKL VAVKERLQQS LAGGPALGLS VSNKNKSQDT
TNKPQSNAPE QSLPVNCVSE LRKRSPSIVT SNQGRVLQKA KEWEMKKT
