ID   QNR71_COTJA             Reviewed;         559 AA.
AC   Q90372;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Protein QNR-71;
DE   Flags: Precursor;
GN   Name=QNR-71;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=8670835; DOI=10.1002/j.1460-2075.1996.tb00699.x;
RA   Turque N., Denhez F., Martin P., Planque N., Bailly M., Begue A.,
RA   Stehelin D., Saule S.;
RT   "Characterization of a new melanocyte-specific gene (QNR-71) expressed in
RT   v-myc-transformed quail neuroretina.";
RL   EMBO J. 15:3338-3350(1996).
RN   [2]
RP   SEQUENCE REVISION.
RA   Saule S.;
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Could be involved in melanogenesis.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Melanocyte-specific, restricted to the pigmented
CC       layer of the retina and the epidermis.
CC   -!- DEVELOPMENTAL STAGE: Transcriptionally regulated by MYC in the
CC       transdifferentiation of embryo pigmented epithelial cells. Expression
CC       precedes melanization.
CC   -!- SIMILARITY: Belongs to the PMEL/NMB family. {ECO:0000305}.
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DR   EMBL; X94144; CAA63859.1; -; mRNA.
DR   RefSeq; NP_001310122.1; NM_001323193.1.
DR   AlphaFoldDB; Q90372; -.
DR   ELM; Q90372; -.
DR   PRIDE; Q90372; -.
DR   GeneID; 107309209; -.
DR   KEGG; cjo:107309209; -.
DR   CTD; 10457; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR045219; PKAT.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   PANTHER; PTHR11861; PTHR11861; 1.
DR   Pfam; PF00801; PKD; 1.
DR   SMART; SM00089; PKD; 1.
DR   SUPFAM; SSF49299; SSF49299; 1.
DR   PROSITE; PS50093; PKD; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..559
FT                   /note="Protein QNR-71"
FT                   /id="PRO_0000024715"
FT   TOPO_DOM        23..487
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        488..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        509..559
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          239..326
FT                   /note="PKD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT   REGION          329..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   559 AA;  61714 MW;  81E2793BD64A47DD CRC64;
     MSQAHRHLAL LLPAEAVLCA AAMRFQDVLS NGRTAPVTNH KKIQGWSSDQ NKWNEKLYPF
     WEDNDPRWKD CWKGGKVTTK LVTDSPALVG SNVTFVVTLQ FPKCQKEDDD GNIIYQRNCT
     PDSPAAQDQY VYNWTEWIDN CGWENCTSNH SHNVFPDGKP FPHYPGWRRR NFVYLFHTVG
     QYYQTIGRSS ANFSVNTANI TLGKHIMAVS IYRRGHSTYV PIARASTTYV VTDKIPILVS
     MSQKHDRNIS DSIFIKDSPI TFDVKIHDPS YYLNDSAISY KWNFGDGSGL FVESGATTSH
     TFSLQGNFTL NLTVQAIIPV PCKPVTPTPS LPTPAVTTDA SSNSDPSAPN EMAEDNPDGG
     CHIYRYGYYT AGITIVEGIL EVNIIQMTSI QMTESQAENP LVDFVVTCQG SFPTDVCTAV
     SDPTCQVSQG MVCDPVVVTD ECVLTIRRAF DEPGTYCINI TLGDDTSQAL ASALISVNGG
     SSSGTTKGVF IFLGLLAVFG AIGAFVLYKR YKQYKPIERS AGQAENQEGL SAYVSNFKAF
     FFPKSTERNP LLKSKPGIV