MACO1_DANRE
ID MACO1_DANRE Reviewed; 664 AA.
AC Q2TLY2; Q1L869; Q2TLY0;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Macoilin-1;
DE AltName: Full=Transmembrane protein 57a;
GN Name=Maco1a {ECO:0000312|ZFIN:ZDB-GENE-040426-1097}; Synonyms=tmem57a;
GN ORFNames=si:dkey-264p5.3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000312|EMBL:AAX11927.1}
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.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: May play a role in the regulation of neuronal activity.
CC {ECO:0000250|UniProtKB:Q8N5G2}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q7TQE6};
CC Multi-pass membrane protein {ECO:0000255}. Rough endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the macoilin family. {ECO:0000255}.
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DR EMBL; AY845029; AAX11927.1; -; mRNA.
DR EMBL; AY845031; AAX11929.1; -; mRNA.
DR EMBL; CR954168; CAK10899.2; -; Genomic_DNA.
DR EMBL; CU469458; CAK10899.2; JOINED; Genomic_DNA.
DR EMBL; CU469458; CAX13653.1; -; Genomic_DNA.
DR EMBL; CR954168; CAX13653.1; JOINED; Genomic_DNA.
DR RefSeq; NP_956613.2; NM_200319.2.
DR AlphaFoldDB; Q2TLY2; -.
DR SMR; Q2TLY2; -.
DR STRING; 7955.ENSDARP00000008156; -.
DR PaxDb; Q2TLY2; -.
DR Ensembl; ENSDART00000009149; ENSDARP00000008156; ENSDARG00000005625.
DR GeneID; 393289; -.
DR KEGG; dre:393289; -.
DR CTD; 393289; -.
DR ZFIN; ZDB-GENE-040426-1097; maco1a.
DR eggNOG; KOG1821; Eukaryota.
DR GeneTree; ENSGT00390000016613; -.
DR HOGENOM; CLU_012823_1_0_1; -.
DR InParanoid; Q2TLY2; -.
DR OMA; GENTHAD; -.
DR OrthoDB; 1227984at2759; -.
DR PhylomeDB; Q2TLY2; -.
DR TreeFam; TF324023; -.
DR Reactome; R-DRE-8980692; RHOA GTPase cycle.
DR Reactome; R-DRE-9013106; RHOC GTPase cycle.
DR PRO; PR:Q2TLY2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000005625; Expressed in testis and 26 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IBA:GO_Central.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
DR GO; GO:0023041; P:neuronal signal transduction; IBA:GO_Central.
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; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..664
FT /note="Macoilin-1"
FT /id="PRO_0000408365"
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 206..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 215
FT /note="T -> I (in Ref. 1; AAX11929)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="I -> T (in Ref. 1; AAX11929)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 664 AA; 76082 MW; 5F13BA21BF4EEB3C CRC64;
MKRRNADCSK LRRPLKRNRI TEGIHSSTFL YLKFLVVWAL VLLADFVLEF RFEYLWPFWL
FIRSVYDSFR YQGLAFSVFF VCVAFTSDII CLLFIPKQWL FFAASTYVWV QYVWHTERGV
CLPTVSLWIL FVYIEAAIRF KDLKHFHVDL CRPFAAHCIG YPVVTLGFGF KSYVSYKMRL
RKQKEVQKEN EFYMQLLQQA LPPEQQMLQR QERETEEATS KGMSEADSVL VAQNGTAINK
KLPISLPELE YKEKGKDSAK DKKQQQHSIG INNNILQTVD AKLQDIEYME NHLNAKRLNN
ELGGSAENLF LKEEVGAGGG SAPSKHYKNS SPRSHNSTNG SVPSSSSNRS DKKQKCTGKN
LAPHRDLMEN CIPNNQLSKP DALVRLEQDI KKLKADLQAS RQVEQDLRSQ ISSLSSAERS
MRSELGQLRQ ENELLQNKLH NAVQAKQKDK QTIVQLEKRL KAEQEARAAV EKQLAEEKKR
KKMEEATAAR AVALAAASRG ECTDSLKSRI RELESECKKL THDMKLKEEQ IRELELKAQE
LHKYKENEKD TEVLMSALSA MQDKTQHLEN SLSAETRIKL DLFSALGDAK RQLEIAQGQI
LQKEQEIKEL KQKIAEVMAV MPSITYSAET NNMTPVTPHY SSKFMDTSPS SLDPNASVYQ
PLKK
