ABLM3_MOUSE
ID ABLM3_MOUSE Reviewed; 682 AA.
AC Q69ZX8; Q52KR1; Q6PAI7;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Actin-binding LIM protein 3;
DE Short=abLIM-3;
DE AltName: Full=Actin-binding LIM protein family member 3;
GN Name=Ablim3; Synonyms=Kiaa0843;
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].
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17194709; DOI=10.1074/jbc.m607549200;
RA Barrientos T., Frank D., Kuwahara K., Bezprozvannaya S., Pipes G.C.T.,
RA Bassel-Duby R., Richardson J.A., Katus H.A., Olson E.N., Frey N.;
RT "Two novel members of the ABLIM protein family, ABLIM-2 and -3, associate
RT with STARS and directly bind F-actin.";
RL J. Biol. Chem. 282:8393-8403(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; SER-280; SER-502 AND
RP THR-542, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-282; SER-290;
RP SER-337; SER-372; SER-373; SER-379; SER-502; SER-503; THR-542; SER-566;
RP SER-575 AND SER-606, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
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).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-630, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May act as scaffold protein. May stimulate ABRA activity and
CC ABRA-dependent SRF transcriptional activity.
CC -!- SUBUNIT: Directly interacts with F-actin and ABRA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, lung and liver. In the
CC brain, highly expressed in the olfactory bulb. In the hippocampus,
CC expressed selectively in the CA2 and CA3 fields. In the cerebellum,
CC expressed in internal granular cells. {ECO:0000269|PubMed:17194709}.
CC -!- DEVELOPMENTAL STAGE: At 15.5 dpc, expressed in skeletal muscle. Down-
CC regulated in adult skeletal muscle. {ECO:0000269|PubMed:17194709}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32318.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173040; BAD32318.1; ALT_INIT; mRNA.
DR EMBL; BC060275; AAH60275.1; -; mRNA.
DR EMBL; BC094229; AAH94229.1; -; mRNA.
DR CCDS; CCDS37839.1; -.
DR RefSeq; NP_001157963.1; NM_001164491.1.
DR RefSeq; NP_941051.2; NM_198649.3.
DR AlphaFoldDB; Q69ZX8; -.
DR BMRB; Q69ZX8; -.
DR SMR; Q69ZX8; -.
DR BioGRID; 235467; 2.
DR IntAct; Q69ZX8; 2.
DR MINT; Q69ZX8; -.
DR STRING; 10090.ENSMUSP00000041243; -.
DR iPTMnet; Q69ZX8; -.
DR PhosphoSitePlus; Q69ZX8; -.
DR SwissPalm; Q69ZX8; -.
DR jPOST; Q69ZX8; -.
DR MaxQB; Q69ZX8; -.
DR PaxDb; Q69ZX8; -.
DR PeptideAtlas; Q69ZX8; -.
DR PRIDE; Q69ZX8; -.
DR ProteomicsDB; 286063; -.
DR Antibodypedia; 1195; 164 antibodies from 22 providers.
DR DNASU; 319713; -.
DR Ensembl; ENSMUST00000049378; ENSMUSP00000041243; ENSMUSG00000032735.
DR Ensembl; ENSMUST00000166783; ENSMUSP00000125836; ENSMUSG00000032735.
DR GeneID; 319713; -.
DR KEGG; mmu:319713; -.
DR UCSC; uc008fct.2; mouse.
DR CTD; 22885; -.
DR MGI; MGI:2442582; Ablim3.
DR VEuPathDB; HostDB:ENSMUSG00000032735; -.
DR eggNOG; KOG1044; Eukaryota.
DR GeneTree; ENSGT00950000182850; -.
DR HOGENOM; CLU_001357_12_3_1; -.
DR InParanoid; Q69ZX8; -.
DR OMA; XCAGCKE; -.
DR OrthoDB; 192350at2759; -.
DR PhylomeDB; Q69ZX8; -.
DR TreeFam; TF318042; -.
DR BioGRID-ORCS; 319713; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Ablim3; mouse.
DR PRO; PR:Q69ZX8; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q69ZX8; protein.
DR Bgee; ENSMUSG00000032735; Expressed in embryonic brain and 195 other tissues.
DR Genevisible; Q69ZX8; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR Gene3D; 1.10.950.10; -; 1.
DR InterPro; IPR028449; ABLIM3.
DR InterPro; IPR032402; AbLIM_anchor.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24213:SF0; PTHR24213:SF0; 1.
DR Pfam; PF16182; AbLIM_anchor; 1.
DR Pfam; PF00412; LIM; 4.
DR Pfam; PF02209; VHP; 1.
DR SMART; SM00132; LIM; 4.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF47050; SSF47050; 1.
DR PROSITE; PS51089; HP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; LIM domain; Metal-binding; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; Zinc.
FT CHAIN 1..682
FT /note="Actin-binding LIM protein 3"
FT /id="PRO_0000075703"
FT DOMAIN 21..80
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 80..140
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 149..208
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 208..268
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 614..682
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 372..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O94929"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94929"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 376
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O94929"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94929"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94929"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 542
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 630
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 381
FT /note="T -> I (in Ref. 2; AAH60275)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 682 AA; 77630 MW; 44E7E59BD850F9CE CRC64;
MNTSIPYQQS PYSPRGGSNV IQCYRCGDTC KGEVVRVHNN HFHIRCFTCQ VCGCGLAQSG
FFFKNQEYIC TQDYQQLYGT RCDSCRDFIT GEVISALGRT YHPKCFVCSL CRKPFPIGDK
VTFSGKECVC QTCSQSMTSS KPIKIRGPSH CAGCKEEIKH GQSLLALDKQ WHVSCFKCQT
CSVILTGEYI SKDGVPYCES DYHSQFGIKC ETCDRYISGR VLEAGGKHYH PTCARCVRCH
QMFTEGEEMY LTGSEVWHPI CKQAARAEKK LKHRRTSETS ISPPGSSIGS PNRVICAKVD
NEILNYKDLA ALPKVKSIYE VQRPDLISYE PHSRYTSDEM LERCGYGESL GTLSPYSQDI
YENLDLRQRR ASSPGYIDSP TYSRQGMSPT FSRSPHYYRS GPESGRSSPY HSQLDVRSST
PTSYQAPKHF HIPAGESNIY RKPPIYKRHG DLSTATKSKT SEDISQASKY SPAYSPDPYY
ASESEYWTYH GSPKVPRARR FSSGGEEEDF DRSMHKLQSG IGRLILKEEM KARSSSYADP
WTPPRSSTSS REALHTTGYE MSFNGSPRSH YLADSDPLIS KSASLPAYRR NGLHRTPSAD
LFHYDSMNAV NWGMREYKIY PYELLLVTTR GRNRLPKDVD RTRLERHLSQ EEFYQVFGMT
ISEFERLALW KRNELKKQAR LF
