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MA7D3_MOUSE
ID   MA7D3_MOUSE             Reviewed;         876 AA.
AC   A2AEY4; Q0VF65; Q8C7V9; Q8C857; Q8CDD4;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=MAP7 domain-containing protein 3;
GN   Name=Map7d3; Synonyms=Mdp3 {ECO:0000303|PubMed:22142902}, Mtap7d3;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-519 (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 22-876 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head, Embryonic stem cell, and Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-876.
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   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=22142902; DOI=10.4161/cc.10.22.18106;
RA   Sun X., Shi X., Liu M., Li D., Zhang L., Liu X., Zhou J.;
RT   "Mdp3 is a novel microtubule-binding protein that regulates microtubule
RT   assembly and stability.";
RL   Cell Cycle 10:3929-3937(2011).
CC   -!- FUNCTION: Promotes the assembly and stability of microtubules.
CC       {ECO:0000250|UniProtKB:Q8IWC1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:Q8IWC1}. Note=Localizes to the microtubules
CC       throughout mitosis. {ECO:0000250|UniProtKB:Q8IWC1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2AEY4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AEY4-2; Sequence=VSP_028500;
CC   -!- TISSUE SPECIFICITY: High expression in lung, skeletal muscle, brain,
CC       and kidney, with much weaker expression in spleen, small intestine,
CC       liver, and heart. {ECO:0000269|PubMed:22142902}.
CC   -!- SIMILARITY: Belongs to the MAP7 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI18964.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC26846.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC33317.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAM26746.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL671998; CAM26745.1; -; Genomic_DNA.
DR   EMBL; AL671998; CAM26746.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK030211; BAC26846.1; ALT_INIT; mRNA.
DR   EMBL; AK048385; BAC33317.1; ALT_INIT; mRNA.
DR   EMBL; AK049164; BAC33580.1; -; mRNA.
DR   EMBL; BC118963; AAI18964.1; ALT_INIT; mRNA.
DR   CCDS; CCDS40982.1; -. [A2AEY4-1]
DR   RefSeq; NP_796267.2; NM_177293.3. [A2AEY4-1]
DR   AlphaFoldDB; A2AEY4; -.
DR   SMR; A2AEY4; -.
DR   BioGRID; 236396; 1.
DR   STRING; 10090.ENSMUSP00000110414; -.
DR   iPTMnet; A2AEY4; -.
DR   PhosphoSitePlus; A2AEY4; -.
DR   jPOST; A2AEY4; -.
DR   MaxQB; A2AEY4; -.
DR   PaxDb; A2AEY4; -.
DR   PeptideAtlas; A2AEY4; -.
DR   PRIDE; A2AEY4; -.
DR   ProteomicsDB; 287290; -. [A2AEY4-1]
DR   ProteomicsDB; 287291; -. [A2AEY4-2]
DR   Antibodypedia; 51701; 20 antibodies from 10 providers.
DR   DNASU; 320923; -.
DR   Ensembl; ENSMUST00000114766; ENSMUSP00000110414; ENSMUSG00000067878. [A2AEY4-1]
DR   GeneID; 320923; -.
DR   KEGG; mmu:320923; -.
DR   UCSC; uc009tgp.1; mouse. [A2AEY4-1]
DR   UCSC; uc009tgq.1; mouse. [A2AEY4-2]
DR   CTD; 79649; -.
DR   MGI; MGI:2445051; Map7d3.
DR   VEuPathDB; HostDB:ENSMUSG00000067878; -.
DR   eggNOG; ENOG502SDH7; Eukaryota.
DR   GeneTree; ENSGT00950000182941; -.
DR   HOGENOM; CLU_016292_0_0_1; -.
DR   InParanoid; A2AEY4; -.
DR   OMA; WSWEGSA; -.
DR   OrthoDB; 441248at2759; -.
DR   PhylomeDB; A2AEY4; -.
DR   TreeFam; TF332273; -.
DR   BioGRID-ORCS; 320923; 3 hits in 71 CRISPR screens.
DR   PRO; PR:A2AEY4; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; A2AEY4; protein.
DR   Bgee; ENSMUSG00000067878; Expressed in epiblast (generic) and 40 other tissues.
DR   ExpressionAtlas; A2AEY4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0046785; P:microtubule polymerization; ISS:UniProtKB.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..876
FT                   /note="MAP7 domain-containing protein 3"
FT                   /id="PRO_0000306813"
FT   REGION          30..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          742..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          58..136
FT                   /evidence="ECO:0000255"
FT   COILED          549..578
FT                   /evidence="ECO:0000255"
FT   COILED          626..658
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        42..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..664
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        768..783
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWC1"
FT   MOD_RES         483
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWC1"
FT   VAR_SEQ         202..231
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_028500"
FT   CONFLICT        217
FT                   /note="S -> C (in Ref. 2; BAC26846)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   876 AA;  98230 MW;  BF11198ABE63267C CRC64;
     MADPTFAATS SSTSFRGLHE RLVAMTQELA EERRHKRGIN SSAGANKRSS STPDGSVLKN
     DVKQQLAKER REQQKRQQEA NKEKQLLEKE QKAKLQYEKQ LEEKHRKLKE QKEKDQRRQA
     SAEEKRKQKQ AEDTEKFKAV VSRTLERCNR IDQRQKRWSW EGGVMNADKS GKLENKRSSS
     LSRKDNRLHP RGDMQHVDNT PGMTKYVFRY VTAPVFSSDE IKSSAMFCKP SAKTPVAAKL
     EKITTKKLDA SLRGHVEGLS MMNIEIPPKI TIEVPSPPKL EESSEADAEV RLQTMDDISK
     VKEDASQKVD IKVPTDENIA RHPKPNVEEL SPVSVDTSSS VELSSIVSVN SSPSLSTGSF
     SFGSVEISPV VSIDASLETN IDTSPELSMD SGNTKVASEI KTEAPLQARG ESRLEASVEG
     QPEANVEGSP KNPEIDKRNI NLTTKKQPLC HIPCYRWPSS SALGCRPPSP LKALQTRKIR
     PPSPIPVSSK LSTKTSLSYK ITPVQNVLYV PNSLGVIATK KETIQKYPIK KEFGNRSMPS
     AEAIKKAFIQ IRHAAYEQSK NEKERLQKEE TKQRIARKPE IMAEKLDKVP AEGSLPCQDE
     QQDKNPTKTF LESPEVQKAE LQKGDSAMMK SRDSAEQRKK EQENILQHWQ ERLERRKASE
     ISFSSEDEAD DEGESEDSLE IFPSGGKMLS MKLKKFHKYA KTKPQKLVFL QSGTDEVDTN
     KNVYFNGDMK AVKQKDPKYS MIQGKGSKLS AKKPPTRPIR SRKTKEGSTA IRPTQSASSN
     PNHKWVCDKV IDFNQTPFLK TTLTKSNKES PADSKIACQG PQAHLDHRKR TKSVSVPLTN
     VLSHLHITGR ASNLEHPFAS VYSRLAFGKE AEESDV
 
 
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