MAP4_RAT
ID MAP4_RAT Reviewed; 1057 AA.
AC Q5M7W5; Q75NR5; Q75NR6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Microtubule-associated protein 4;
DE Short=MAP-4;
GN Name=Map4;
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 MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 653-827 (ISOFORMS 1 AND 2).
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 [3]
RP PHOSPHORYLATION AT SER-915.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9108484; DOI=10.1016/s0092-8674(00)80208-1;
RA Drewes G., Ebneth A., Preuss U., Mandelkow E.-M., Mandelkow E.;
RT "MARK - a novel family of protein kinases that phosphorylate microtubule-
RT associated proteins and trigger microtubule disruption.";
RL Cell 89:297-308(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-509; SER-515;
RP SER-520; SER-522; SER-618; THR-659; SER-902; SER-915 AND SER-978, AND
RP IDENTIFICATION BY 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: Non-neuronal microtubule-associated protein. Promotes
CC microtubule assembly (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SEPTIN2; this interaction impedes tubulin-
CC binding. Interacts with TRAF3IP1 (By similarity). Interacts with KNSTRN
CC (By similarity). {ECO:0000250|UniProtKB:P27546,
CC 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=2;
CC Name=1;
CC IsoId=Q5M7W5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5M7W5-2; Sequence=VSP_032080;
CC -!- PTM: Phosphorylation on Ser-761 negatively regulates MAP4 activity to
CC promote microtubule assembly. Phosphorylated at serine residues in K-X-
CC G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1 or
CC MARK2), causing detachment from microtubules, and their disassembly.
CC {ECO:0000269|PubMed:9108484}.
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DR EMBL; BC088405; AAH88405.1; -; mRNA.
DR EMBL; AB175782; BAD14292.1; -; mRNA.
DR EMBL; AB175783; BAD14293.1; -; mRNA.
DR RefSeq; NP_001019449.1; NM_001024278.1. [Q5M7W5-1]
DR AlphaFoldDB; Q5M7W5; -.
DR BioGRID; 266360; 3.
DR IntAct; Q5M7W5; 2.
DR MINT; Q5M7W5; -.
DR STRING; 10116.ENSRNOP00000053011; -.
DR iPTMnet; Q5M7W5; -.
DR PhosphoSitePlus; Q5M7W5; -.
DR jPOST; Q5M7W5; -.
DR PRIDE; Q5M7W5; -.
DR GeneID; 367171; -.
DR UCSC; RGD:1564359; rat. [Q5M7W5-1]
DR CTD; 4134; -.
DR RGD; 1564359; Map4.
DR VEuPathDB; HostDB:ENSRNOG00000020748; -.
DR eggNOG; KOG2418; Eukaryota.
DR HOGENOM; CLU_012370_0_0_1; -.
DR InParanoid; Q5M7W5; -.
DR OrthoDB; 716848at2759; -.
DR PhylomeDB; Q5M7W5; -.
DR PRO; PR:Q5M7W5; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000020748; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; Q5M7W5; baseline and differential.
DR Genevisible; Q5M7W5; RN.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0005930; C:axoneme; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; ISO:RGD.
DR GO; GO:0072686; C:mitotic spindle; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0051301; P:cell division; ISO:RGD.
DR GO; GO:0051294; P:establishment of spindle orientation; ISO:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0051012; P:microtubule sliding; ISO:RGD.
DR GO; GO:0007052; P:mitotic spindle organization; ISO:RGD.
DR GO; GO:1902856; P:negative regulation of non-motile cilium assembly; ISO:RGD.
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; 2.
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 Isopeptide bond; Microtubule; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT CHAIN 2..1057
FT /note="Microtubule-associated protein 4"
FT /id="PRO_0000323721"
FT REPEAT 897..927
FT /note="Tau/MAP 1"
FT REPEAT 928..958
FT /note="Tau/MAP 2"
FT REPEAT 959..990
FT /note="Tau/MAP 3"
FT REGION 49..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1057
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 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27546"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 450
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27546"
FT MOD_RES 497
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 506
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27546"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 546
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 659
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 902
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 915
FT /note="Phosphoserine; by MARK1"
FT /evidence="ECO:0000305|PubMed:9108484,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 916
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1050
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT MOD_RES 1056
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT CROSSLNK 812
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P27816"
FT VAR_SEQ 674..747
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15840943"
FT /id="VSP_032080"
SQ SEQUENCE 1057 AA; 110301 MW; C306932206B242CB CRC64;
MADLSLVDAL TEPPPEIEGE IKRDFMAALE AEPYDDIVGE TVEKTEFIPL LDGDEKSGNS
ESKRKPCVDT SQVEDIPSSK PTLLANGDHG VEGNNTTGSP TDFLVENVDY EDYQNSQSWP
EDASFCFQPQ QVLDTNQADP FNVHHDDGLA DLLFVSSGPT NASAFIEENN PLEDSYGVLP
CDSFAPTAVV SQEWSVGAPD SPHSEPCVSP EVTIETAQPA TELSKAVDLE SVKEQLPAKA
LEMMAGQTTD AVPSKESEGS PDTDAAPGPD TDVTLTKDIE ESSSPDVISA NVTQPFTESD
MFLTQEMELL IGTEAAQVKD TMSSVEPDIS SAKNTAPPTE EETVPGKDMT FPKEAETALP
IEMDLAPPED VALPKETELE LAPAAGTAPL SETEVALAKD EEPSTGIPAA QEMLLSSETE
VVLPSDSIMT LTKEVTVPLE AAGPLVSDMT AILETEMTLG GGTATPTETK LGKVKDMAPL
PESEVALGKD VVTLPETKVT EFNNVTPLSE EEVASIKDVS PSPETETAKN ADLHSGTELT
LDNSMTPPSD PALPLETKVA TVQIKDKETV QTQEELSEDS QLESVQLEGQ SAVPPCTISP
EPVKAADQKS TLPVDEGSPL EKLEQKETSG SQPPELCSGV SRQEEGKAAV GLTGNDIATP
PNKELPPSPE KKAKPLATTQ PAKTSTSKAK IQPTSLPKQP APTTSGGLNK KPMSLASGSV
PAAPHKRPAA ATATARPSTL PARDLKPKPI TETKVAEKRT SPSKPSSAPA LRPGPKTTPT
ISKATSPSTL VSTGSSSRSP STTLPKRPTT TKTEGKPADV KRMTAKSATA DLSRSKTTSA
SSVKRNTTPT GATPPAGMAS TRVKPMSAPC RSSVALSVDK KPTSTKPSSS APRVSRLATT
VSAPDLKSVR SKVGSTENMK HQPGGGRVQI QNKKVDISKV SSKCGSKANI KHKPGGGDVK
IESQKLNFKE KAQAKVGSLD NVGHLPAGGT VKTEGGGSEA PPCPGPPAGE EPAIPEAAPD
AGAPTSASGL SGHTTLSGGG DQREPQTLDS QIQETSI
