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MACOI_RAT
ID   MACOI_RAT               Reviewed;         664 AA.
AC   Q4V7D3; Q2TLZ0;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Macoilin;
DE   AltName: Full=Macoilin-1;
DE   AltName: Full=Transmembrane protein 57;
GN   Name=Maco1 {ECO:0000312|RGD:1561685}; Synonyms=Tmem57;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
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.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; AY845021; AAX11919.1; -; mRNA.
DR   EMBL; BC097999; AAH97999.1; -; mRNA.
DR   RefSeq; NP_001020870.2; NM_001025699.2.
DR   AlphaFoldDB; Q4V7D3; -.
DR   SMR; Q4V7D3; -.
DR   STRING; 10116.ENSRNOP00000029925; -.
DR   GlyGen; Q4V7D3; 4 sites.
DR   iPTMnet; Q4V7D3; -.
DR   PhosphoSitePlus; Q4V7D3; -.
DR   PaxDb; Q4V7D3; -.
DR   PRIDE; Q4V7D3; -.
DR   Ensembl; ENSRNOT00000079536; ENSRNOP00000069310; ENSRNOG00000056156.
DR   GeneID; 313618; -.
DR   KEGG; rno:313618; -.
DR   CTD; 55219; -.
DR   RGD; 1561685; Maco1.
DR   eggNOG; KOG1821; Eukaryota.
DR   GeneTree; ENSGT00390000016613; -.
DR   HOGENOM; CLU_012823_1_0_1; -.
DR   InParanoid; Q4V7D3; -.
DR   OMA; KIHEMEY; -.
DR   OrthoDB; 1227984at2759; -.
DR   PhylomeDB; Q4V7D3; -.
DR   Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR   Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR   PRO; PR:Q4V7D3; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000056156; Expressed in testis and 19 other tissues.
DR   Genevisible; Q4V7D3; RN.
DR   GO; GO:0030424; C:axon; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; ISO:RGD.
DR   GO; GO:0044306; C:neuron projection terminus; ISO:RGD.
DR   GO; GO:0031965; C:nuclear membrane; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0030867; C:rough endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0007420; P:brain development; ISO:RGD.
DR   GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Nucleus; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..664
FT                   /note="Macoilin"
FT                   /id="PRO_0000070271"
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          252..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..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        630..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"
FT   CONFLICT        301
FT                   /note="D -> V (in Ref. 1; AAX11919)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   664 AA;  76082 MW;  EFF1DDCB58A8BD33 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
     KKLSTALPEI EYREKGKEKD KDAKKHNLGI NNNNILQPVD SKIQEIEYME NHINSKRLNN
     DLVGSTENLL KEDSCTASSK NYKNASGVVN SSPRSHSATN GSIPSSSSKN EKKQRCTSKG
     PSAHKDLMEN CIPNNQLSKP DALVRLEQDI KKLKADLQAS RQVEQELRSQ ISSLSSTERG
     IRSEMGQLRQ ENELLQNKLH NAVQMKQKDK QNISQLEKRL KAEQEARGFV EKQLMEEKKR
     KKLEEATAAR AVAFAAASRG ECTETLRSRI RELEAEGKKL TMDLKVKEEQ IRELELKVQE
     LRKYKENEKD TEVLMSALSA MQDKTQHLEN SLSAETRIKL DLFSALGDAK RQLEIAQGQI
     LQKDQEIKDL KQKIAEVMAV MPSITYSAAT SPLSPVSPHY SSKFVETSPS GLDPNASVYQ
     PLKK
 
 
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