MAP1S_BOVIN
ID MAP1S_BOVIN Reviewed; 1066 AA.
AC A6QQ70;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Microtubule-associated protein 1S;
DE Short=MAP-1S;
DE Contains:
DE RecName: Full=MAP1S heavy chain;
DE Contains:
DE RecName: Full=MAP1S light chain;
GN Name=MAP1S;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Microtubule-associated protein that mediates aggregation of
CC mitochondria resulting in cell death and genomic destruction (MAGD).
CC Plays a role in anchoring the microtubule organizing center to the
CC centrosomes. Binds to DNA. Plays a role in apoptosis. Involved in the
CC formation of microtubule bundles (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of a heavy and a light chain. Interacts with
CC microtubules and actin. Both MAP1S heavy and light chains interact with
CC microtubules. MAP1S light chain interacts with actin. Interacts (via C-
CC terminus) with GAN (via Kelch domains). Interacts with ESR1, LRPPRC,
CC RASSF1, microtubules and VCY2 (By similarity). Interacts with ESR1,
CC LRPPRC, RASSF1, microtubules and VCY2. Interacts with WDR47 (via N-
CC terminus of light chain) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q66K74}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250|UniProtKB:Q66K74}. Note=Detected in perinuclear
CC punctate network corresponding to mitochondrial aggregates and in the
CC nucleus in cells exhibiting apoptosis. Associated specifically with
CC microtubules stabilized by paclitaxel and colocalizes with RASSF1. In
CC interphase cells, shows a diffuse cytoplasmic staining with partial
CC localization to the microtubules. During the different stages of
CC mitosis detected at the spindle microtubules. Detected in filopodia-
CC like protrusions and synapses (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The N-terminus of the heavy chain associates with the C-
CC terminus of the light chain to form the heterodimer complex. Its C-
CC terminal part of the heavy chain interacts with ESR1 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAP1 family. {ECO:0000305}.
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DR EMBL; BC149678; AAI49679.1; -; mRNA.
DR RefSeq; NP_001095584.1; NM_001102114.1.
DR AlphaFoldDB; A6QQ70; -.
DR STRING; 9913.ENSBTAP00000019513; -.
DR PaxDb; A6QQ70; -.
DR PRIDE; A6QQ70; -.
DR GeneID; 527829; -.
DR KEGG; bta:527829; -.
DR CTD; 55201; -.
DR eggNOG; KOG3592; Eukaryota.
DR InParanoid; A6QQ70; -.
DR OrthoDB; 86642at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031114; P:regulation of microtubule depolymerization; IBA:GO_Central.
DR InterPro; IPR026074; MAP1.
DR InterPro; IPR027322; MAP1S.
DR PANTHER; PTHR13843; PTHR13843; 2.
DR PANTHER; PTHR13843:SF11; PTHR13843:SF11; 2.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Cytoskeleton; DNA-binding; Microtubule; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1066
FT /note="Microtubule-associated protein 1S"
FT /id="PRO_0000311376"
FT CHAIN 1..836
FT /note="MAP1S heavy chain"
FT /id="PRO_0000311377"
FT CHAIN 837..1066
FT /note="MAP1S light chain"
FT /id="PRO_0000311378"
FT REGION 1..804
FT /note="Necessary for the microtubule-organizing center
FT localization"
FT /evidence="ECO:0000250"
FT REGION 462..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..1066
FT /note="Necessary for interaction with RASSF1"
FT /evidence="ECO:0000250"
FT REGION 720..973
FT /note="Necessary for association with microtubules"
FT /evidence="ECO:0000250"
FT REGION 758..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1066
FT /note="Necessary for association with actin"
FT /evidence="ECO:0000250"
FT REGION 974..998
FT /note="Necessary for the mitochondrial aggregation and
FT genome destruction"
FT /evidence="ECO:0000250"
FT COMPBIAS 467..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..581
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..851
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
FT MOD_RES 647
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C5W1"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C052"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
SQ SEQUENCE 1066 AA; 112472 MW; 67A5E4630AAD677E CRC64;
MAATVAGSGA AEVPSSLLLV VGGECGCRGL LAYVLEELER GIRSWDIDPG VCSLDEQLKV
FVSRHSATFS SIVKGQRSLH HRGDTLETLV LLNPSDKSLC DELRNLLLDT ASHKLLVLAG
PCLEETGELL LQTGGFSPRH FLQVLGDKEI RDLLASTPPP AAPPKLTITC PTFGDWARLA
PEVPGLQGVL HLRLNPPVQL PASEGLREFL EYVAESLEPP SPFELLEPPA SVGLLRLARP
CCYIFPGGLG DAAFFAVNGF TVLVNGGSNP KSSFWKLVRH LDRVDAVLVT HAGADSLPGL
NSLLRRKLAE RDEAAAGGGS GDDRLRRLIS PNLGVVFLNA RAAASRLVRG EDEAELALSL
LSQLGITPVP LNRGPLPAEP TVLFQKMGVG RLDMYVLHPP SAATTDHTLA SVCALLVWHP
AGPSEKVVRV LFPGCTPPAR LLDGLVHLQH LGFLREPVVT PQDMAGPRRA ESKESVASRD
SLRREGRTTV PSRPTQERPG VARKDSPRTE APRRAEKEAR PSREVKKDPR PSAPRTQPRE
VRRAASAVVS GKNVGAQVAP KTRRAPNTPR PGVPPAENGP RSPPSFRSGE ASPPTEACSS
PAPQLVATPS QESSLDLGLS PAGEEGGSLE EKTLELLLAA STPEPCTPSP AGAQQGPTES
SGPLSLSPLR GGEPGPDASP TVTTPSLPAE VGSPHSTEVD ESLSVSFEQV LPPPAAAASE
AGLSLPLCGP RVRRSASPHD VDLCLVSPCE FEHRKAVPMA PAPVSPGSSN DSSARSQERA
GAPGGAEETP PTSVSESLPT LSDSDPLPAA PGTADSDEDT EGFGVPRRDP LPDPLKIPPP
LPTPPSICMV DPEMLPPEQA RLKGGGSRTR KPLTRPSSGT TPPKATPVTA AKIKGLASGD
RASRPLSARS EPSDKGNRAS LSRKPSVPKT TTRGPSGSAG SRSGGSAAPP GSPVYLDLAY
LPSGGSARLV DEEFFRRVRA LCYVISGQDQ HKEEGMRAVL DALLAGKQQW DRQLQVTLIP
TFDSVAMHEW YEETHTRHQA LGITVLGSNS TVSMQDEAFP ACKVEF
