MACOI_BOVIN
ID MACOI_BOVIN Reviewed; 664 AA.
AC Q2TLZ3;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Macoilin;
DE AltName: Full=Transmembrane protein 57;
GN Name=MACO1; Synonyms=TMEM57;
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].
RA Huang C.-H., Chen Y.;
RT "Identification of macoilin as a novel membrane-associated coiled-coil
RT tetraspanin protein.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the regulation of neuronal activity.
CC {ECO:0000250|UniProtKB:Q8N5G2}.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein
CC {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P91193}; Multi-
CC pass membrane protein {ECO:0000255}. Note=Detected in the nucleus
CC membrane of non-neuronal cells and in axonal outgrowths of neuronal
CC cells. {ECO:0000250|UniProtKB:Q7TQE6}.
CC -!- SIMILARITY: Belongs to the macoilin family. {ECO:0000305}.
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DR EMBL; AY845018; AAX11916.1; -; mRNA.
DR RefSeq; NP_001033736.1; NM_001038647.1.
DR AlphaFoldDB; Q2TLZ3; -.
DR SMR; Q2TLZ3; -.
DR STRING; 9913.ENSBTAP00000003890; -.
DR PaxDb; Q2TLZ3; -.
DR PRIDE; Q2TLZ3; -.
DR Ensembl; ENSBTAT00000003890; ENSBTAP00000003890; ENSBTAG00000002988.
DR GeneID; 540726; -.
DR KEGG; bta:540726; -.
DR CTD; 55219; -.
DR VEuPathDB; HostDB:ENSBTAG00000002988; -.
DR VGNC; VGNC:36098; MACO1.
DR eggNOG; KOG1821; Eukaryota.
DR GeneTree; ENSGT00390000016613; -.
DR HOGENOM; CLU_012823_1_0_1; -.
DR InParanoid; Q2TLZ3; -.
DR OMA; KIHEMEY; -.
DR OrthoDB; 1227984at2759; -.
DR TreeFam; TF324023; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000002988; Expressed in spermatid and 102 other tissues.
DR ExpressionAtlas; Q2TLZ3; baseline and differential.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044306; C:neuron projection terminus; IEA:Ensembl.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0023041; P:neuronal signal transduction; ISS:UniProtKB.
DR InterPro; IPR019130; Macoilin.
DR PANTHER; PTHR47464:SF3; PTHR47464:SF3; 1.
DR Pfam; PF09726; Macoilin; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..664
FT /note="Macoilin"
FT /id="PRO_0000070264"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 253..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5G2"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5G2"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5G2"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5G2"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 664 AA; 76118 MW; C622A3D035EBD781 CRC64;
MKRRNADCSK LRRPLKRNRI TEGIYGSTFL YLKFLVVWAL VLLADFVLEF RFEYLWPFWL
FIRSVYDSFR YQGLAFSVFF VCVAFTSNII CLLFIPIQWL FFAASTYVWV QYVWHTERGV
CLPTVSLWIL FVYIEAAIRF KDLKNFHVDL CRPFAAHCIG YPVVTLGFGF KSYVSYKMRL
RKQKEVQKEN EFYMQLLQQA LPPEQQMLQK QEKEAEEAAK GLPDMDSSIL IHHNGGIPAN
KKLSTTLPEI EYREKGKEKD KDAKKHNLGI NNNNILQPVD SKIQEIEYME NHINSKRLNN
DLVGSTENLL KEDSCTASSK NYKNASGVVN SSPRSHSATN GSIPSSSSKN EKKQKCTSKS
PSAHKDLMEN CIPNNQLSKP DALVRLEQDI KKLKADLQAS RQVEQELRSQ ISSLSSTERG
IRSEMGQLRQ ENELLQNKLH NAVQMKQKDK QNISQLEKKL KAEQEARSFV EKQLMEEKKR
KKLEEATAAR AVAFAAASRG ECTETLRNRI RELEAEGKKL TMDMKVKEDQ IRELELKVQE
LRKYKENEKD TEVLMSALSA MQDKTQHLEN SLSAETRIKL DLFSALGDAK RQLEIAQGQI
LQKDQEIKDL KQKIAEVMAV MPSITYSAAA SPLSPVSPHY SSKFVETSPS GLDPNASVYQ
PLKK
