ID   JKIP1_BOVIN             Reviewed;         626 AA.
AC   A6QR54;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Janus kinase and microtubule-interacting protein 1;
GN   Name=JAKMIP1;
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=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Associates with microtubules and may play a role in the
CC       microtubule-dependent transport of the GABA-B receptor. May play a role
CC       in JAK1 signaling and regulate microtubule cytoskeleton rearrangements
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Forms a complex with GABBR1 and KIF5B/kinesin-1.
CC       Interacts with JAK1 and TYK2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC       Note=Colocalizes with the microtubule network. Localizes to the cell
CC       body and neurites of hippocampal neurons where it accumulates in
CC       granules. Localizes to the tail and to a lower extent to the head of
CC       sperm cells (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the JAKMIP family. {ECO:0000305}.
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DR   EMBL; BC150119; AAI50120.1; -; mRNA.
DR   RefSeq; NP_001095721.1; NM_001102251.1.
DR   RefSeq; XP_010804597.1; XM_010806295.2.
DR   RefSeq; XP_010804598.1; XM_010806296.2.
DR   RefSeq; XP_015327186.1; XM_015471700.1.
DR   AlphaFoldDB; A6QR54; -.
DR   SMR; A6QR54; -.
DR   STRING; 9913.ENSBTAP00000055002; -.
DR   PaxDb; A6QR54; -.
DR   PRIDE; A6QR54; -.
DR   GeneID; 540970; -.
DR   KEGG; bta:540970; -.
DR   CTD; 152789; -.
DR   eggNOG; ENOG502QS6X; Eukaryota.
DR   HOGENOM; CLU_020294_2_0_1; -.
DR   InParanoid; A6QR54; -.
DR   OrthoDB; 727914at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0050811; F:GABA receptor binding; IBA:GO_Central.
DR   GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR024836; JAKMIP.
DR   InterPro; IPR031994; JAKMIP_C.
DR   PANTHER; PTHR18935; PTHR18935; 1.
DR   Pfam; PF16034; JAKMIP_CC3; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Microtubule;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..626
FT                   /note="Janus kinase and microtubule-interacting protein 1"
FT                   /id="PRO_0000323007"
FT   REGION          1..365
FT                   /note="Mediates association with microtubules"
FT                   /evidence="ECO:0000250"
FT   REGION          365..626
FT                   /note="Mediates interaction with TYK2 and GABBR1"
FT                   /evidence="ECO:0000250"
FT   REGION          452..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          19..254
FT                   /evidence="ECO:0000255"
FT   COILED          284..413
FT                   /evidence="ECO:0000255"
FT   COILED          490..604
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        466..480
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         382
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96N16"
FT   MOD_RES         470
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96N16"
SQ   SEQUENCE   626 AA;  73271 MW;  A28342247981FA4D CRC64;
     MSKKGRSKGE KPEMEMDPVQ MANEELRAKL TSIQIEFQQE KSKVGKLRER LQEAKLEREQ
     EQRRHTAYIS ELRAKLHEEK TKELQALREV LIRQHEQEAA RTAKIKEGEL QRLQATLNVL
     RDGAADKVKT ALLADARDEA RRAFDGERLR LQQEILELKA ARKQAEEALS NCMQADKTKA
     ADLRAAYQAH QDEVHRIKRE CERDIRRLMD EIKGKDRVIL ALEKELGVQT GQTQKLLLQK
     EALDEQLVQV REAERYHGSP KRELPPGIGD MAELMGVQDQ HMDERDVRRF QLKIAELNSV
     IRKLEDRNTL LADERNELLK RSRETEVQLK PLVEKNKRMN KKNEDLLQSI QRMEEKIKNL
     TRENVEMKEK LSAQASLKRH TSLNDLSLTR DEQEIEFLRL QVLEQQHVID DLSLERERLL
     RSRRHRGKGL KPPKKHVVET FFGFDEESVD SETLSETSCN TDRTDRAPAT PEEDLDDTTT
     REEADLRFCQ LTREYQALQR AYALLQEQVG GTLDAEREAR TREQLQADLL RCQAKIEDLE
     KLLVEKGQDS KWVEEKQLLI RTNQDLLEKI YRLEMEENQL KNEMQDAKDQ NELLEFRVLE
     LEVRDSICCK LSNGADILFE PKLKFM