ID   F168B_RAT               Reviewed;         194 AA.
AC   D4AEP3;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Myelin-associated neurite-outgrowth inhibitor;
DE            Short=Mani;
GN   Name=Fam168b;
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 [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, INTERACTION WITH CDC27, AND GLYCOSYLATION.
RX   PubMed=20716133; DOI=10.1111/j.1582-4934.2010.01134.x;
RA   Mishra M., Akatsu H., Heese K.;
RT   "The novel protein MANI modulates neurogenesis and neurite-cone growth.";
RL   J. Cell. Mol. Med. 15:1713-1725(2011).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=22771904; DOI=10.1016/j.febslet.2012.06.043;
RA   Mishra M., Lee S., Lin M.K., Yamashita T., Heese K.;
RT   "Characterizing the neurite outgrowth inhibitory effect of Mani.";
RL   FEBS Lett. 586:3018-3023(2012).
CC   -!- FUNCTION: Inhibitor of neuronal axonal outgrowth. Acts as a negative
CC       regulator of CDC42 and STAT3 and a positive regulator of STMN2.
CC       Positive regulator of CDC27. {ECO:0000269|PubMed:20716133}.
CC   -!- SUBUNIT: May form homodimers (By similarity). May interact with DAZAP2,
CC       FAM168A, PRDX6, RBM6, TMTC1 and YPEL2 (By similarity). Interacts with
CC       CDC27 (PubMed:20716133). {ECO:0000250|UniProtKB:A1KXE4,
CC       ECO:0000269|PubMed:20716133}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:22771904}. Cell membrane
CC       {ECO:0000269|PubMed:22771904}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:22771904}. Cell projection, axon
CC       {ECO:0000269|PubMed:22771904}. Note=In cortical neurons, predominantly
CC       found at perinuclear regions. Expressed in neuronal cell bodies and
CC       axonal fibers. {ECO:0000269|PubMed:22771904}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20716133}.
CC   -!- SIMILARITY: Belongs to the FAM168 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH473965; EDL99300.1; -; Genomic_DNA.
DR   RefSeq; NP_001258063.1; NM_001271134.1.
DR   AlphaFoldDB; D4AEP3; -.
DR   BioGRID; 605005; 3.
DR   IntAct; D4AEP3; 4.
DR   MINT; D4AEP3; -.
DR   STRING; 10116.ENSRNOP00000065566; -.
DR   GlyGen; D4AEP3; 1 site.
DR   PeptideAtlas; D4AEP3; -.
DR   GeneID; 690188; -.
DR   KEGG; rno:690188; -.
DR   UCSC; RGD:1583985; rat.
DR   CTD; 130074; -.
DR   RGD; 1583985; Fam168b.
DR   VEuPathDB; HostDB:ENSRNOG00000023467; -.
DR   eggNOG; ENOG502QQDS; Eukaryota.
DR   HOGENOM; CLU_065824_1_0_1; -.
DR   InParanoid; D4AEP3; -.
DR   OMA; AMYAPHI; -.
DR   OrthoDB; 1348118at2759; -.
DR   PhylomeDB; D4AEP3; -.
DR   TreeFam; TF331128; -.
DR   PRO; PR:D4AEP3; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Proteomes; UP000234681; Chromosome 9.
DR   Bgee; ENSRNOG00000023467; Expressed in frontal cortex and 19 other tissues.
DR   Genevisible; D4AEP3; RN.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR029247; FAM168A/MANI.
DR   PANTHER; PTHR31844; PTHR31844; 1.
DR   Pfam; PF14944; TCRP1; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Cell projection; Cytoplasm; Glycoprotein;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..194
FT                   /note="Myelin-associated neurite-outgrowth inhibitor"
FT                   /id="PRO_0000418109"
FT   TOPO_DOM        1..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        42..141
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        164..194
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:A1KXE4"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A1KXE4"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   194 AA;  20194 MW;  B59FCF5407B00518 CRC64;
     MNPVYSPGSS GVPYANAKGI GYPAGFPVGY AAAPAYSPNM YPGANPTFQT GYTPGTPYKV
     SCSPTSGAVP PYSSSPNPYQ TAVYPVRSAY PQQSPYAQQG TYYTQPLYAA PPHVIHHTTV
     VQPNGMPATV YPAPIPPPRG SGVTMGMVAG TTMAMSAGTL LTAHSPTPVA PHPVTVPTYR
     APGTPTYSYV PPQW