MA7D1_MOUSE
ID MA7D1_MOUSE Reviewed; 846 AA.
AC A2AJI0; Q80TI3; Q8CIL3; Q8VCG2; Q91YQ4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=MAP7 domain-containing protein 1;
GN Name=Map7d1; Synonyms=Kiaa1187, Mtap7d1;
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] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 220-846 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 291-846 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544; SER-548 AND SER-552, AND
RP 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-544; SER-548 AND THR-554, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53; SER-315; SER-479;
RP SER-496; SER-544; SER-548 AND SER-552, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AJI0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AJI0-2; Sequence=VSP_028489;
CC -!- SIMILARITY: Belongs to the MAP7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16081.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH19977.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC65744.3; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it is derived from pre-RNA.; Evidence={ECO:0000305};
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DR EMBL; AL732624; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016081; AAH16081.1; ALT_INIT; mRNA.
DR EMBL; BC019977; AAH19977.1; ALT_INIT; mRNA.
DR EMBL; BC023677; AAH23677.1; -; mRNA.
DR EMBL; AK122462; BAC65744.3; ALT_SEQ; Transcribed_RNA.
DR CCDS; CCDS18646.1; -. [A2AJI0-1]
DR RefSeq; NP_659190.3; NM_144941.3. [A2AJI0-1]
DR RefSeq; XP_006503175.1; XM_006503112.3.
DR AlphaFoldDB; A2AJI0; -.
DR SMR; A2AJI0; -.
DR BioGRID; 232845; 8.
DR IntAct; A2AJI0; 3.
DR MINT; A2AJI0; -.
DR STRING; 10090.ENSMUSP00000054338; -.
DR iPTMnet; A2AJI0; -.
DR PhosphoSitePlus; A2AJI0; -.
DR EPD; A2AJI0; -.
DR jPOST; A2AJI0; -.
DR MaxQB; A2AJI0; -.
DR PaxDb; A2AJI0; -.
DR PeptideAtlas; A2AJI0; -.
DR PRIDE; A2AJI0; -.
DR ProteomicsDB; 287288; -. [A2AJI0-1]
DR ProteomicsDB; 287289; -. [A2AJI0-2]
DR Antibodypedia; 31646; 74 antibodies from 17 providers.
DR DNASU; 245877; -.
DR Ensembl; ENSMUST00000061143; ENSMUSP00000054338; ENSMUSG00000028849. [A2AJI0-1]
DR GeneID; 245877; -.
DR KEGG; mmu:245877; -.
DR UCSC; uc008usy.1; mouse. [A2AJI0-1]
DR CTD; 55700; -.
DR MGI; MGI:2384297; Map7d1.
DR VEuPathDB; HostDB:ENSMUSG00000028849; -.
DR eggNOG; ENOG502QPJP; Eukaryota.
DR GeneTree; ENSGT00950000182941; -.
DR InParanoid; A2AJI0; -.
DR OMA; TKEDTVH; -.
DR OrthoDB; 738080at2759; -.
DR PhylomeDB; A2AJI0; -.
DR TreeFam; TF332273; -.
DR BioGRID-ORCS; 245877; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Map7d1; mouse.
DR PRO; PR:A2AJI0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AJI0; protein.
DR Bgee; ENSMUSG00000028849; Expressed in triceps brachii and 258 other tissues.
DR ExpressionAtlas; A2AJI0; baseline and differential.
DR Genevisible; A2AJI0; MM.
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:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR InterPro; IPR008604; MAP7_fam.
DR Pfam; PF05672; MAP7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..846
FT /note="MAP7 domain-containing protein 1"
FT /id="PRO_0000306808"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 130..224
FT /evidence="ECO:0000255"
FT COILED 414..443
FT /evidence="ECO:0000255"
FT COILED 599..740
FT /evidence="ECO:0000255"
FT COMPBIAS 26..57
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..499
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 554
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 818
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT CROSSLNK 462
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q3KQU3"
FT VAR_SEQ 249..285
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028489"
FT CONFLICT 123..125
FT /note="PAS -> SAY (in Ref. 2; AAH23677)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 846 AA; 93276 MW; 3B4EEDAFEAC93C56 CRC64;
MESGPRVEPG PGAPAAVLAR IPQEPRPSPE GDPSPPPPPT PMSALVPDTP PDTPPALKTA
TNPKQLPLEP GNPTGQISPQ PAPPQEECPS SEAKSRGPTP TATGPREAKP SRRSSQPSPT
TVPASDSPPA KQDVKKAGER HKLAKERREE RAKYLAAKKA VWLEKEEKAK ALREKQLQER
RRRLEEQRLK AEQRRAALEE RQRQKLEKNK ERYEAAIQRS VKKTWAEIRQ QRWSWAGALH
HSSPGRKTSG SRCSVSAVNL PKHVDSIINK RLSKSSATLW NSPSRNRSLQ LSAWESSIVD
RLMTPTLSFL ARSRSAVTLP RNGRDQGRGS GPGRRPTRAR AGASLAPGPH PDRTHPSAAV
PVCPRSASAS PLTPCSAPRS AHRCTPSGER PERRKPGAGG SPALARRRLE ATPVQKKEKK
DKERENEKEK SALARERNLK KRQSLPASIR PRLSTGSELS PKSKARPSSP STTWHRPASP
CPSPGPGHAL PPKPPSPRGT TASPKGRVRR KEEAKESPSP SGPEDKNHRK SRAAEEKEPA
APASPAPSPV PSPTPAQPQK EQSSTQIPAE TAVPAVPAAP TAPPTAAPSV TPSKPMAGTT
DREEATRLLA EKRRQAREQR EREEQERKLQ AERDKRMREE QLAREAEARA EREAEARRRE
EQEAREKAQA EQEEQERLQK QKEEAEARSR EEAERQRQER EKHFQKEEQE RQERRKRLEE
IMKRTRKSEA AETKKQDAKE TAANNSGPDP VKAVETRPSG LQKDSMQKEE LAPQEPQWSL
PSKEMPGSLV NGLQPLPAHQ ENGFSPKGTA GDKSLGRTAE GLLPFAEAEA FLKKAVVQPP
QVTEVL
