EMAL1_RAT
ID EMAL1_RAT Reviewed; 814 AA.
AC Q4V8C3;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Echinoderm microtubule-associated protein-like 1;
DE Short=EMAP-1;
GN Name=Eml1;
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 MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP 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: Modulates the assembly and organization of the microtubule
CC cytoskeleton, and probably plays a role in regulating the orientation
CC of the mitotic spindle and the orientation of the plane of cell
CC division. Required for normal proliferation of neuronal progenitor
CC cells in the developing brain and for normal brain development. Does
CC not affect neuron migration per se. {ECO:0000250|UniProtKB:Q05BC3}.
CC -!- SUBUNIT: Homotrimer; self-association is mediated by the N-terminal
CC coiled coil (By similarity). Does not interact with EML3 (By
CC similarity). Binds repolymerizing microtubules (By similarity). Binds
CC unpolymerized tubulins via its WD repeat region (By similarity).
CC Interacts with TASOR (By similarity). {ECO:0000250|UniProtKB:O00423,
CC ECO:0000250|UniProtKB:Q05BC3, ECO:0000250|UniProtKB:Q9HC35}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05BC3}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q05BC3}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q05BC3}. Note=Detected
CC in cytoplasmic punctae. Co-localizes with microtubules. Enriched in
CC perinuclear regions during interphase and in the region of spindle
CC microtubules during metaphase. Enriched at the midzone during telophase
CC and cytokinesis. Detected at growth cones in neurons.
CC {ECO:0000250|UniProtKB:Q05BC3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4V8C3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4V8C3-2; Sequence=VSP_024479;
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.
CC {ECO:0000250|UniProtKB:O00423}.
CC -!- DOMAIN: The N-terminal coiled coil is required for association with
CC microtubules. {ECO:0000250|UniProtKB:O00423}.
CC -!- SIMILARITY: Belongs to the WD repeat EMAP family. {ECO:0000305}.
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DR EMBL; AABR03049402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03049711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03050272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC097450; AAH97450.1; -; mRNA.
DR RefSeq; NP_001020912.1; NM_001025741.1. [Q4V8C3-2]
DR AlphaFoldDB; Q4V8C3; -.
DR SMR; Q4V8C3; -.
DR BioGRID; 263717; 1.
DR IntAct; Q4V8C3; 1.
DR iPTMnet; Q4V8C3; -.
DR PhosphoSitePlus; Q4V8C3; -.
DR PaxDb; Q4V8C3; -.
DR PRIDE; Q4V8C3; -.
DR GeneID; 362783; -.
DR KEGG; rno:362783; -.
DR UCSC; RGD:1306374; rat. [Q4V8C3-1]
DR CTD; 2009; -.
DR RGD; 1306374; Eml1.
DR eggNOG; KOG2106; Eukaryota.
DR InParanoid; Q4V8C3; -.
DR OrthoDB; 271572at2759; -.
DR PhylomeDB; Q4V8C3; -.
DR PRO; PR:Q4V8C3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR005108; HELP.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF03451; HELP; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 10.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..814
FT /note="Echinoderm microtubule-associated protein-like 1"
FT /id="PRO_0000284387"
FT REPEAT 260..309
FT /note="WD 1"
FT REPEAT 314..357
FT /note="WD 2"
FT REPEAT 362..399
FT /note="WD 3"
FT REPEAT 408..445
FT /note="WD 4"
FT REPEAT 449..488
FT /note="WD 5"
FT REPEAT 492..529
FT /note="WD 6"
FT REPEAT 534..571
FT /note="WD 7"
FT REPEAT 577..612
FT /note="WD 8"
FT REPEAT 616..654
FT /note="WD 9"
FT REPEAT 663..700
FT /note="WD 10"
FT REPEAT 708..767
FT /note="WD 11"
FT REPEAT 774..813
FT /note="WD 12"
FT REGION 77..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..814
FT /note="Tandem atypical propeller in EMLs"
FT /evidence="ECO:0000250"
FT COILED 31..72
FT /evidence="ECO:0000255"
FT COMPBIAS 89..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024479"
SQ SEQUENCE 814 AA; 89802 MW; CF8DD37A5057BD0D CRC64;
MEDGFSSYSS LYDTSSLLQF CNDDSASAAS SMEISDRIAS LEQRVQMQED DIQLLKSALA
DVVRRLNITE EQQAVLNRKG PTKARPLGQT LPLRTTVNNG TVLPKKPSAS LPSPSGSRKE
MVVPVTKSIN RTSSSERVSP GGRRESSGDS KGSRNRTGST SSSSSGKKNS ESKPKEPTFS
PEEGYVKMFL RGRPVTMYMP KDQVDSYSLE AKAELPTKRL KLEWVYGYRG RDCRNNLYLL
PTGETVYFIA SVVVLYNVEE QLQRHYAGHN DDVKCLAVHP DRITIATGQV AGTSKDGKQL
PPHVRIWDSV TLNTLHVIGI GFFDRAVTCI AFSKSNGGSH LCAVDDSNDH VLSVWDWQRE
ERLADVKCSN EAVFAADFHP TDTNIIVTCG KSHLYFWTLE GNSLNKKQGL FEKQEKPKFV
LCVTFSENGD TITGDSSGNI LVWGKGTNRI SYAVQGAHEG GIFALCMLRD GTLVSGGGKD
RRLISWNGNY QKLHKAEIPE QFGPIRTVAE GKGNVILIGT TRNFVLQGTL TGDFTPITQG
HTDELWGLAI HASKPQFLTC GHDKHATLWD AVGHRPVWDK IIEDPAQSSG FHPSGSVVAV
GTLTGRWFVF DTETKDLVTV HTDGNEQLSV MRYSPDGNFL AIGSHDNCIY IYGVSDNGRK
YTRVGKCSGH SSFITHLDWS VNSQFLVSNS GDYEILYWVP SACKQVVSVE TTRDIEWATY
TCTLGFHVFG VWPEGSDGTD INAVCRAHEK KLLSTGDDFG KVHLFSYPCS QFRAPSHIYS
GHSSHVTNVD FLCEDSHLIS TGGKDTSIMQ WRVI
