TXLNA_MOUSE
ID TXLNA_MOUSE Reviewed; 554 AA.
AC Q6PAM1; Q6P1E5;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Alpha-taxilin;
GN Name=Txlna; Synonyms=Txln;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515 AND SER-523, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Liver, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be involved in intracellular vesicle traffic and
CC potentially in calcium-dependent exocytosis in neuroendocrine cells.
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds to the C-terminal coiled coil region of syntaxin family
CC members STX1A, STX3A and STX4A, but not when these proteins are
CC complexed with SNAP25, VAMP2 or STXBP1, suggesting that it interacts
CC with syntaxins that do not form the SNARE complex. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PAM1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PAM1-2; Sequence=VSP_011833, VSP_011834;
CC -!- SIMILARITY: Belongs to the taxilin family. {ECO:0000305}.
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DR EMBL; BC060227; AAH60227.1; -; mRNA.
DR EMBL; BC065115; AAH65115.1; -; mRNA.
DR CCDS; CCDS38887.1; -. [Q6PAM1-1]
DR RefSeq; NP_001005506.2; NM_001005506.3. [Q6PAM1-1]
DR RefSeq; NP_001186624.1; NM_001199695.1. [Q6PAM1-1]
DR RefSeq; XP_006502722.1; XM_006502659.3. [Q6PAM1-1]
DR AlphaFoldDB; Q6PAM1; -.
DR SMR; Q6PAM1; -.
DR BioGRID; 224938; 3.
DR IntAct; Q6PAM1; 1.
DR STRING; 10090.ENSMUSP00000081285; -.
DR iPTMnet; Q6PAM1; -.
DR PhosphoSitePlus; Q6PAM1; -.
DR EPD; Q6PAM1; -.
DR jPOST; Q6PAM1; -.
DR MaxQB; Q6PAM1; -.
DR PaxDb; Q6PAM1; -.
DR PeptideAtlas; Q6PAM1; -.
DR PRIDE; Q6PAM1; -.
DR ProteomicsDB; 298071; -. [Q6PAM1-1]
DR ProteomicsDB; 298072; -. [Q6PAM1-2]
DR Antibodypedia; 31239; 154 antibodies from 29 providers.
DR Ensembl; ENSMUST00000046425; ENSMUSP00000042153; ENSMUSG00000053841. [Q6PAM1-1]
DR Ensembl; ENSMUST00000084264; ENSMUSP00000081285; ENSMUSG00000053841. [Q6PAM1-1]
DR GeneID; 109658; -.
DR KEGG; mmu:109658; -.
DR UCSC; uc008uxx.2; mouse. [Q6PAM1-1]
DR CTD; 200081; -.
DR MGI; MGI:105968; Txlna.
DR VEuPathDB; HostDB:ENSMUSG00000053841; -.
DR eggNOG; KOG1850; Eukaryota.
DR GeneTree; ENSGT00940000158303; -.
DR HOGENOM; CLU_025501_3_0_1; -.
DR InParanoid; Q6PAM1; -.
DR OMA; VTEAPCC; -.
DR PhylomeDB; Q6PAM1; -.
DR TreeFam; TF318595; -.
DR Reactome; R-MMU-449836; Other interleukin signaling.
DR BioGRID-ORCS; 109658; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Txlna; mouse.
DR PRO; PR:Q6PAM1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6PAM1; protein.
DR Bgee; ENSMUSG00000053841; Expressed in manus and 229 other tissues.
DR ExpressionAtlas; Q6PAM1; baseline and differential.
DR Genevisible; Q6PAM1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; IEA:InterPro.
DR GO; GO:0042113; P:B cell activation; IDA:MGI.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR InterPro; IPR026183; Taxilin_fam.
DR PANTHER; PTHR16127; PTHR16127; 1.
DR Pfam; PF09728; Taxilin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Exocytosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..554
FT /note="Alpha-taxilin"
FT /id="PRO_0000189422"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 186..491
FT /evidence="ECO:0000255"
FT COMPBIAS 136..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40222"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 362..409
FT /note="LLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFT ->
FT VRLRPQGCGGAGRKWAGFWLSSIYFLWMGEILPAQSSNCLSRQQSESR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011833"
FT VAR_SEQ 410..554
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011834"
SQ SEQUENCE 554 AA; 62369 MW; 5CFDD86C4E744D06 CRC64;
MKNQDKKNGP AKHSNSKGSP GQREAGPEGA HGRPRQTAPG AEAEGSTSQA PGKTEGARAK
AAQPGALCDV SEELSRQLED ILSTYCVDNN QGGPAEEGAQ GEPTEPEDTE KSRTYAARNG
EPEPGIPVVN GEKETSKGEP GTEEIRASDE VGDRDHRRPQ EKKKAKGLGK EITLLMQTLN
TLSTPEEKLA ALCKKYAELL EEHRNSQKQM KLLQKKQSQL VQEKDHLRGE HSKAVLARSK
LESLCRELQR HNRSLKEEGV QRAREEEEKR KEVTSHFQVT LNDIQLQMEQ HNERNSKLRQ
ENMELAERLK KLIEQYELRE EHIDKVFKHK DLQQQLVDAK LQQAQEMLKE AEERHQREKE
FLLKEAVESQ RMCELMKQQE THLKQQLALY TEKFEEFQNT LSKSSEVFTT FKQEMEKMTK
KIKKLEKETT MYRSRWESSN KALLEMAEEK TVRDKELEGL QVKIQRLEKL CRALQTERND
LNKRVQDLTA GGITDIGSER RPEATTASKE QGVESPGAQP ASSPRATDAP CCSGAPSTGT
AGQTGPGEPT PATA
