MACO2_DANRE
ID MACO2_DANRE Reviewed; 699 AA.
AC Q2TLY1; B7ZUY4;
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-2 {ECO:0000312|EMBL:AAX11928.1};
DE AltName: Full=Transmembrane protein 57b;
GN Name=maco1b {ECO:0000312|ZFIN:ZDB-GENE-040426-1188}; Synonyms=tmem57b;
GN ORFNames=si:dkey-9g4.5, zgc:63610;
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:AAX11928.1}
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).
RN [3] {ECO:0000312|EMBL:AAX11928.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI71392.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q7TQE6}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q7TQE6}. Rough endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P91193}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the macoilin family. {ECO:0000255}.
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DR EMBL; AY845030; AAX11928.1; -; mRNA.
DR EMBL; BX465191; CAX13214.1; -; Genomic_DNA.
DR EMBL; BC171392; AAI71392.1; -; mRNA.
DR RefSeq; NP_956757.2; NM_200463.2.
DR AlphaFoldDB; Q2TLY1; -.
DR SMR; Q2TLY1; -.
DR STRING; 7955.ENSDARP00000069055; -.
DR PaxDb; Q2TLY1; -.
DR PRIDE; Q2TLY1; -.
DR Ensembl; ENSDART00000074567; ENSDARP00000069055; ENSDARG00000012741.
DR GeneID; 393435; -.
DR KEGG; dre:393435; -.
DR CTD; 393435; -.
DR ZFIN; ZDB-GENE-040426-1188; maco1b.
DR eggNOG; KOG1821; Eukaryota.
DR GeneTree; ENSGT00390000016613; -.
DR InParanoid; Q2TLY1; -.
DR OMA; WHTDKGV; -.
DR OrthoDB; 1227984at2759; -.
DR PhylomeDB; Q2TLY1; -.
DR TreeFam; TF324023; -.
DR PRO; PR:Q2TLY1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000012741; Expressed in blastula and 20 other tissues.
DR ExpressionAtlas; Q2TLY1; baseline.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
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 Cell projection; Endoplasmic reticulum; Glycoprotein; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..699
FT /note="Macoilin-2"
FT /id="PRO_0000408366"
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 219..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 226
FT /note="Missing (in Ref. 3; AAI71392)"
FT /evidence="ECO:0000305"
FT CONFLICT 275..276
FT /note="Missing (in Ref. 3; AAI71392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 699 AA; 78344 MW; 96F5EE8A5EC4B4C9 CRC64;
MKRRNADCSK LRRPLKRNRI TEGIYGSTFL YLKFLVVWAL VLLADFVLEF RFEYLWPFWL
FIRSVYDSFR YQGLAFSVFF VCVAFTSDII CLLFIPVQWL FFAASTYVWV QYVWHTERGV
CLPTVSLWIL FVYIEAAIRF KDLKHFHVDL CRPFAAHCIG YPVVTLGFGF KSYVSYKMRL
RKQKEVQKEN EFYMQLLQQA LPPEQQLIQR QEREAEEAAA AAAAAASKSI HDVDSPAVAQ
NGSAGGKKPS SNTLPELEYR EKERGKNESK KQHNHNQNHH SSTSSSILPS VDNKAQEMEY
MENHVNSKRL SSSDLLGSTE NLLKDEHSSS SSSSTSSNSN KNYKNASGGG GGGGSSSPRG
HGTANGSVPS SSGPSSSASS SSKGDRKQKY GGGKNSASHR DPVENCIPNN QLSKPEALVR
LEQDVKKLKA DLQASRQTEQ DLRSQLGSLG TSERSIRSEL GQLRQENELL QNKLHNAVQA
KQKDKQTLGQ LEKRLKAEQE ARAAAEKLLA EEKKRKKLEE ATAARAVALA AATRGECTES
LRRRISELEA ECKKLTLDIK VKEDQIRELE LKVQELHKYK ENEKDTEVLM SALSAMQDKT
QHLENSLSAE TRIKLDLFSA LGDAKRQLEI AQGQILQKDQ EIKDLKQKIA EVMAVMPSVV
YSADTGSMTP VTPHYSSKFM DTSPSGLDPN ASVYQPLKK
