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MAP7_CHICK
ID   MAP7_CHICK              Reviewed;         725 AA.
AC   Q5ZIA2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Ensconsin;
DE   AltName: Full=Microtubule-associated protein 7;
DE            Short=MAP-7;
GN   Name=MAP7; ORFNames=RCJMB04_28m17;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Microtubule-stabilizing protein that may play an important
CC       role during reorganization of microtubules during polarization and
CC       differentiation of epithelial cells.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC       Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MAP7 family. {ECO:0000305}.
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DR   EMBL; AJ720882; CAG32541.1; -; mRNA.
DR   RefSeq; NP_001026243.1; NM_001031072.1.
DR   AlphaFoldDB; Q5ZIA2; -.
DR   SMR; Q5ZIA2; -.
DR   STRING; 9031.ENSGALP00000022497; -.
DR   PaxDb; Q5ZIA2; -.
DR   PRIDE; Q5ZIA2; -.
DR   GeneID; 421689; -.
DR   KEGG; gga:421689; -.
DR   CTD; 9053; -.
DR   VEuPathDB; HostDB:geneid_421689; -.
DR   eggNOG; ENOG502QTDQ; Eukaryota.
DR   InParanoid; Q5ZIA2; -.
DR   OrthoDB; 738080at2759; -.
DR   PhylomeDB; Q5ZIA2; -.
DR   PRO; PR:Q5ZIA2; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   InterPro; IPR030707; MAP7.
DR   InterPro; IPR008604; MAP7_fam.
DR   PANTHER; PTHR15073:SF4; PTHR15073:SF4; 1.
DR   Pfam; PF05672; MAP7; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Reference proteome.
FT   CHAIN           1..725
FT                   /note="Ensconsin"
FT                   /id="PRO_0000255951"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          71..131
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..137
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..421
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..539
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..602
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   725 AA;  82313 MW;  4784F5F7BBD57220 CRC64;
     MAEAAGRSGG RRRRAAEGSK TQDKKVASGQ SNTGTKPDHP PILKVDDRQR LARERREERE
     KQLAARETVW LEREERARQH YEKHLEERKK KLEEQRLKEE GRRAAVEEKR RQRIEEDKER
     HEAVVRRTIE RSQKPKQKQN RWSWGGALHS RINNSDPDRR SVSTMNLSKH VDPVINKRLS
     SSSATLLNSS DRARRLQLSP WESSIVSRLL TPTHSFLARS KSTAALSGDA ASCSPISPLS
     YKTMSCRNSA DRAKLFASTD AVGRRRTHLA GTDKKEKERD HLSSNFSANL KGGHFSSNPK
     ARSPAPSPVW HASKSLPSLA GTLKQITSPP GSSKVPSTQA RPPSPGNIRP VKKDTKPENE
     KKRAEKEAEK ANEERTEGSK ETSAGTGESA NQEELAVQAE DAQAASPSLP PAPPALSPPP
     APMKTSAGTT DPEEATRLLS EKRRLAREQR EREEQERRER EELERQKKEE LSQRIAEERA
     RREEEEARRQ EAERKRKDAE EEREKEERLR RQAEEREQKE REEMERIQKQ KEEEARLREE
     AERIRLEREK HFQREEQERL ERKKRLEEIM KRTRRVEAVD KKPNDQQNGH ISKANNTGEA
     VITSPAPPME PSGGPQLQHA TQSPHSGKPV TCTHTIVSHQ PPMNMDSNLN PEKNTEENGM
     SMQNDNFEEI INLPIGSKPS RLDALNNDGS DSPGIPLNPI LAFEDKGTLL PQVDSVQTHQ
     TAEVI
 
 
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