EMAL2_RAT
ID EMAL2_RAT Reviewed; 649 AA.
AC Q6P6T4; Q8VIM8;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Echinoderm microtubule-associated protein-like 2;
DE Short=EMAP-2;
GN Name=Eml2; Synonyms=Emap2;
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 [MRNA] (ISOFORM 2), INTERACTION WITH GRID1 AND GRID2,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11829466; DOI=10.1006/bbrc.2002.6413;
RA Ly C.D., Roche K.W., Lee H.K., Wenthold R.J.;
RT "Identification of rat EMAP, a delta-glutamate receptor binding protein.";
RL Biochem. Biophys. Res. Commun. 291:85-90(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
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).
CC -!- FUNCTION: Tubulin binding protein that inhibits microtubule nucleation
CC and growth, resulting in shorter microtubules.
CC {ECO:0000250|UniProtKB:O95834}.
CC -!- SUBUNIT: Interacts with GRID2 and may also interact with GRID1
CC (PubMed:11829466). Interacts with EML3 (By similarity). Binds
CC unpolymerized tubulins via its WD repeat region (By similarity).
CC {ECO:0000250|UniProtKB:O95834, ECO:0000269|PubMed:11829466}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O95834}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:O95834}. Note=Colocalizes with the microtubule
CC cytoskeleton. Colocalizes with the mitotic spindle.
CC {ECO:0000250|UniProtKB:O95834}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P6T4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P6T4-2; Sequence=VSP_024481;
CC -!- TISSUE SPECIFICITY: Widely expressed in both brain and peripheral
CC tissues, including brainstem and enrichment in the postsynaptic
CC density, PSD. {ECO:0000269|PubMed:11829466}.
CC -!- DOMAIN: Contains a tandem atypical propeller in EMLs (TAPE) domain. The
CC N-terminal beta-propeller is formed by canonical WD repeats; in
CC contrast, the second beta-propeller contains one blade that is formed
CC by discontinuous parts of the polypeptide chain (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat EMAP family. {ECO:0000305}.
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DR EMBL; AF335571; AAL33537.1; -; mRNA.
DR EMBL; BC062038; AAH62038.1; -; mRNA.
DR PIR; JC7808; JC7808.
DR RefSeq; NP_620276.1; NM_138921.1.
DR AlphaFoldDB; Q6P6T4; -.
DR SMR; Q6P6T4; -.
DR BioGRID; 251413; 1.
DR IntAct; Q6P6T4; 1.
DR STRING; 10116.ENSRNOP00000046691; -.
DR iPTMnet; Q6P6T4; -.
DR PhosphoSitePlus; Q6P6T4; -.
DR jPOST; Q6P6T4; -.
DR PaxDb; Q6P6T4; -.
DR PRIDE; Q6P6T4; -.
DR GeneID; 192360; -.
DR KEGG; rno:192360; -.
DR CTD; 24139; -.
DR RGD; 621066; Eml2.
DR VEuPathDB; HostDB:ENSRNOG00000030127; -.
DR eggNOG; KOG2106; Eukaryota.
DR HOGENOM; CLU_011754_2_0_1; -.
DR InParanoid; Q6P6T4; -.
DR OMA; IEDPGRC; -.
DR OrthoDB; 271572at2759; -.
DR PhylomeDB; Q6P6T4; -.
DR PRO; PR:Q6P6T4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000030127; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q6P6T4; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IDA:RGD.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IDA:RGD.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0010968; P:regulation of microtubule nucleation; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR033016; EML2.
DR InterPro; IPR005108; HELP.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR PANTHER; PTHR13720:SF50; PTHR13720:SF50; 1.
DR Pfam; PF03451; HELP; 1.
DR Pfam; PF00400; WD40; 6.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50952; SSF50952; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Microtubule;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..649
FT /note="Echinoderm microtubule-associated protein-like 2"
FT /id="PRO_0000284389"
FT REPEAT 56..93
FT /note="WD 1"
FT REPEAT 97..144
FT /note="WD 2"
FT REPEAT 151..192
FT /note="WD 3"
FT REPEAT 195..234
FT /note="WD 4"
FT REPEAT 241..280
FT /note="WD 5"
FT REPEAT 285..323
FT /note="WD 6"
FT REPEAT 369..406
FT /note="WD 7"
FT REPEAT 410..447
FT /note="WD 8"
FT REPEAT 452..489
FT /note="WD 9"
FT REPEAT 495..535
FT /note="WD 10"
FT REPEAT 564..602
FT /note="WD 11"
FT REPEAT 609..648
FT /note="WD 12"
FT REGION 10..649
FT /note="Tandem atypical propeller in EMLs"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11829466"
FT /id="VSP_024481"
FT CONFLICT 311..312
FT /note="GG -> VW (in Ref. 1; AAL33537)"
FT /evidence="ECO:0000305"
FT CONFLICT 491..492
FT /note="QG -> HC (in Ref. 1; AAL33537)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 649 AA; 70711 MW; BCAEEA4699EEB9A9 CRC64;
MSSFGTGKTK EVIFSMEEGS VKMFLRGRPV PMLIPDELAP TYSLDTRSEL PSSRLKLDWV
YGYRGRDCRA NLYLLPTGEV VYFVASVAVL YSVEEQRQRH YLGHNDDIKC LAVHPDMVTI
ATGQVAGTTK EGKPLPPHVR VWDSVSLSTL HVLGLGVFDR AVCCVAFSKS NGGNLLCAVD
ESNDHVLSVW DWAKESKVVD SKCSNEAVLV ATFHPTDPNL LITCGKSHIY FWSLEGGNLS
KRQGLFEKHE KPKYVLCVTF LEGGDVVTGD SGGNLYVWGK GGNRITQEVL GAHDGGVFAL
CALRDGTLVS GGGRDRRVVL WGSDYSKVQE VEVPEDFGPV RTVAEGRGDT LYVGTTRNSI
LLGSVHTGFS LLVQGHVEEL WGLATHPSRA QFVSCGQDKL VHLWSSETHQ PVWSRSIEDP
ARSAGFHPSG SVLAVGTVTG RWLLLDTDTR DLVAIHTDGN EQISVVSFSP DGAYLAVGSH
DNLVYVYTVD QGGRKVSRLG KCSGHSSFIT HLDWAQDSTC FVTNSGDYEI LYWDAATCKQ
ITSADTVRNV QWATATCVLG FGVFGIWPEG ADGTDINAVA RSHDGNLLVS ADDFGKVHLF
SYPCCQPRAL SHKYGGHSSH VTNVAFLWDD SMVLTTGGKD TSVLQWRVA
