MAP4_BOVIN
ID MAP4_BOVIN Reviewed; 1072 AA.
AC P36225; A7BKA6; Q867A8; Q8MJX2; Q8MJX3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Microtubule-associated protein 4;
DE Short=MAP-4;
DE AltName: Full=Microtubule-associated protein U;
DE Short=MAP-U;
GN Name=MAP4;
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 [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2380192; DOI=10.1016/s0021-9258(18)77426-7;
RA Aizawa H., Emori Y., Murofushi H., Kawasaki H., Sakai H., Suzuki K.;
RT "Molecular cloning of a ubiquitously distributed microtubule-associated
RT protein with Mr 190,000.";
RL J. Biol. Chem. 265:13849-13855(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 320-1072 (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 403-1072 (ISOFORM 3), AND FUNCTION.
RC TISSUE=Adrenal gland;
RX PubMed=12773533; DOI=10.1074/jbc.m302186200;
RA Tokuraku K., Matsushima K., Matui T., Nakagawa H., Katsuki M., Majima R.,
RA Kotani S.;
RT "The number of repeat sequences in microtubule-associated protein 4 affects
RT the microtubule surface properties.";
RL J. Biol. Chem. 278:29609-29618(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 544-1072 (ISOFORM 4).
RC TISSUE=Adrenal medulla;
RX PubMed=15840943; DOI=10.1247/csf.29.111;
RA Matsushima K., Aosaki M., Tokuraku K., Hasan M.R., Nakagawa H., Kotani S.;
RT "Identification of a neural cell specific variant of microtubule-associated
RT protein 4.";
RL Cell Struct. Funct. 29:111-124(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 563-717.
RC TISSUE=Adrenal gland;
RA Matsushima K.;
RT "Bos taurus MAP4 mRNA for microtubule-associated protein 4 transcript
RT variant.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DOMAINS.
RX PubMed=2033072; DOI=10.1016/s0021-9258(18)92896-6;
RA Aizawa H., Emori Y., Mori A., Murofushi H., Sakai H., Suzuki K.;
RT "Functional analyses of the domain structure of microtubule-associated
RT protein-4 (MAP-U).";
RL J. Biol. Chem. 266:9841-9846(1991).
CC -!- FUNCTION: Non-neuronal microtubule-associated protein. Promotes
CC microtubule assembly. {ECO:0000269|PubMed:12773533}.
CC -!- SUBUNIT: Interacts with SEPTIN2; this interaction impedes tubulin-
CC binding (By similarity). Interacts with TRAF3IP1 (By similarity).
CC Interacts with KNSTRN (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P27546, ECO:0000250|UniProtKB:P27816}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P27816}. Cytoplasm, cytoskeleton, microtubule
CC organizing center {ECO:0000250|UniProtKB:P27816}. Note=Recruitment to
CC microtubule is inhibited by microtubules polyglutamylation.
CC {ECO:0000250|UniProtKB:P27816}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P36225-1; Sequence=Displayed;
CC Name=2; Synonyms=R3;
CC IsoId=P36225-2; Sequence=VSP_032061, VSP_032063, VSP_032064;
CC Name=3; Synonyms=R5;
CC IsoId=P36225-3; Sequence=VSP_032062, VSP_032063, VSP_032064;
CC Name=4;
CC IsoId=P36225-4; Sequence=VSP_032060, VSP_032062, VSP_032063,
CC VSP_032064;
CC -!- TISSUE SPECIFICITY: Is distributed ubiquitously among all tissues but
CC amounts are lower in cerebellum and liver.
CC -!- PTM: Phosphorylated at serine residues in K-X-G-S motifs by
CC MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing
CC detachment from microtubules, and their disassembly (By similarity).
CC Phosphorylation on Ser-734 negatively regulates MAP4 activity to
CC promote microtubule assembly. {ECO:0000250}.
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DR EMBL; D90149; BAA14179.1; -; mRNA.
DR EMBL; AB079579; BAC07258.1; -; mRNA.
DR EMBL; AB079580; BAC07259.1; -; mRNA.
DR EMBL; AB354119; BAF75374.1; -; mRNA.
DR EMBL; AB100953; BAC56093.1; -; mRNA.
DR PIR; A37127; A37127.
DR RefSeq; NP_776530.1; NM_174105.2. [P36225-1]
DR AlphaFoldDB; P36225; -.
DR BMRB; P36225; -.
DR STRING; 9913.ENSBTAP00000021045; -.
DR iPTMnet; P36225; -.
DR PaxDb; P36225; -.
DR PeptideAtlas; P36225; -.
DR PRIDE; P36225; -.
DR GeneID; 281295; -.
DR KEGG; bta:281295; -.
DR CTD; 4134; -.
DR eggNOG; KOG2418; Eukaryota.
DR InParanoid; P36225; -.
DR OrthoDB; 716848at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR InterPro; IPR027323; MAP4.
DR InterPro; IPR001084; MAP_tubulin-bd_rpt.
DR PANTHER; PTHR11501:SF16; PTHR11501:SF16; 1.
DR Pfam; PF00418; Tubulin-binding; 3.
DR PROSITE; PS00229; TAU_MAP_1; 3.
DR PROSITE; PS51491; TAU_MAP_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Isopeptide bond; Microtubule; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT CHAIN 2..1072
FT /note="Microtubule-associated protein 4"
FT /id="PRO_0000072750"
FT REPEAT 244..257
FT /note="1"
FT REPEAT 258..271
FT /note="2"
FT REPEAT 272..285
FT /note="3"
FT REPEAT 286..299
FT /note="4"
FT REPEAT 300..313
FT /note="5"
FT REPEAT 314..327
FT /note="6"
FT REPEAT 328..341
FT /note="7"
FT REPEAT 342..355
FT /note="8"
FT REPEAT 384..391
FT /note="9; truncated"
FT REPEAT 392..405
FT /note="10"
FT REPEAT 406..417
FT /note="11"
FT REPEAT 418..431
FT /note="12"
FT REPEAT 432..445
FT /note="13"
FT REPEAT 446..460
FT /note="14"
FT REPEAT 461..474
FT /note="15"
FT REPEAT 475..488
FT /note="16"
FT REPEAT 489..502
FT /note="17"
FT REPEAT 503..516
FT /note="18"
FT REPEAT 517..530
FT /note="19"
FT REPEAT 869..899
FT /note="Tau/MAP 1"
FT REPEAT 938..968
FT /note="Tau/MAP 2"
FT REPEAT 969..1000
FT /note="Tau/MAP 3"
FT REGION 54..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..530
FT /note="19 X 14 AA tandem repeats"
FT REGION 543..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..849
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27546"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 282
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27546"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 416
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 501
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27546"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 800
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 887
FT /note="Phosphoserine; by MARK1"
FT /evidence="ECO:0000250|UniProtKB:Q5M7W5"
FT MOD_RES 888
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 988
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 1060
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 1066
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT CROSSLNK 785
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT VAR_SEQ 649..720
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15840943"
FT /id="VSP_032060"
FT VAR_SEQ 900..937
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12773533"
FT /id="VSP_032061"
FT VAR_SEQ 937
FT /note="K -> KVQIVSKKVSYSHIQSKCGSKDNIKHVPGGGN (in isoform 3
FT and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12773533,
FT ECO:0000303|PubMed:15840943"
FT /id="VSP_032062"
FT VAR_SEQ 1067
FT /note="K -> I (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12773533,
FT ECO:0000303|PubMed:15840943"
FT /id="VSP_032063"
FT VAR_SEQ 1068..1072
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12773533,
FT ECO:0000303|PubMed:15840943"
FT /id="VSP_032064"
SQ SEQUENCE 1072 AA; 111915 MW; E8C17A730989F0D2 CRC64;
MADLSLADAL TEPSPEIEEE IKRDFIATLE AEAFDDVVGE TVGKTDYIPL LDVDEKTGSS
ESKKKPCSDT SQVEGTPSSQ AAVLANGDHG IERNDVTGFP SEFLEEKMAY QGYQNSQNWP
ENTNFCFEPE HMVNPIQTDP FKMHHDDGLE DSLFFPSGTT NTSVFVEQND PLKDTYGMLP
CDTFAPAAVV PQGWSAEAPN LAHLESFTSP EAVPQPLQPT AEPAEKVEMA SGEERAEALE
MMMKLQAADM APSREAEMVL AKDVVPATET GVALAKDMES PTKPDEALVK DVESSIESDM
ALVKDVVLPV QTEETAVKDA ILPTETDVSL DEDLALSTET EVSTAQDILL FKETESIPPV
TMDLASAEGT VPPTDQEMTP VKVAASLSEI EAPLDEDIVS STEIRSAKEI GLSSETEVAL
SREMGLPPET EAILDKDMAA PPETEVIVPV KDMAPSPGIE TTLAKDVAPR QEIEVTLGKD
TVSLPATEMA LGRNVALPPE TEVTLAKDVA QPPETEVNLA NNAALAKFSE AEVVPVPVKD
METAQTQEAT SEDSQLKSLQ DEGQSAVPLM TSPEAVVAMG QKHSLPTDED SVLEELEQKK
PSSQTSELPS ETSGVAKPEE GPPTGSVSGN DITAPPNKEL PPSPEKKTKP LATTQPAKTS
TSKAKTQPTS LPKQTAPTTL GGSNKKPMSL ASGSVPAAPP KRPAAATSRP STLPSKDTKP
KPVAEAKIPE KRVSPSKPAS APAVKPGSKS TQAVPKAPAT ATLASPGSTS RNLSTPLPKR
PTAIKTEGKP AEIKKMATKS APADLSRPKS TTTSSVKKST TVPGTAPPAG APSRARPTAT
PPRPSGTPPV DKKPTAAKPT SSAPRLGRVA ANASAPDLKN VRSKVGSTEN IKHQPGGGRA
KVEKKTEAAA PARKPEPNAV TKAAGPIGNA QKPPTGKVQI QNKKVDISKV SSKCGSKANI
KHKPGGGDVK IESQKLNFKE KAQAKVGSLD NVGHLPAGGA VKTEGGGSEA PPCPGPPAGE
ELAIPEAAPE AGAPASASGL SGHTTLAGGG DQREAQTLDS QIQETSKWLG LA
