ID   CNIH2_CHICK             Reviewed;         160 AA.
AC   Q401C0;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Protein cornichon homolog 2;
DE            Short=CNIH-2;
DE   AltName: Full=Cornichon family AMPA receptor auxiliary protein 2;
DE   AltName: Full=Cornichon-like protein;
GN   Name=CNIH2; Synonyms=CNIL;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HBEGF, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=17229890; DOI=10.1091/mbc.e06-08-0733;
RA   Hoshino H., Uchida T., Otsuki T., Kawamoto S., Okubo K., Takeichi M.,
RA   Chisaka O.;
RT   "Cornichon-like protein facilitates secretion of HB-EGF and regulates
RT   proper development of cranial nerves.";
RL   Mol. Biol. Cell 18:1143-1152(2007).
CC   -!- FUNCTION: Regulates the trafficking and gating properties of AMPA-
CC       selective glutamate receptors (AMPARs) (By similarity). Plays an
CC       important role in the proper development of cranial nerves by
CC       facilitating the secretion of HBEGF. {ECO:0000250,
CC       ECO:0000269|PubMed:17229890}.
CC   -!- SUBUNIT: Interacts with HBEGF. {ECO:0000269|PubMed:17229890}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the odd-numbered neuromeres (r3 and
CC       r5) of the developing hindbrain. {ECO:0000269|PubMed:17229890}.
CC   -!- SIMILARITY: Belongs to the cornichon 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; AB232677; BAE20186.1; -; mRNA.
DR   RefSeq; NP_001028673.1; NM_001033501.1.
DR   AlphaFoldDB; Q401C0; -.
DR   SMR; Q401C0; -.
DR   BioGRID; 689033; 1.
DR   GeneID; 613230; -.
DR   CTD; 254263; -.
DR   VEuPathDB; HostDB:geneid_421323; -.
DR   InParanoid; Q401C0; -.
DR   PhylomeDB; Q401C0; -.
DR   PRO; PR:Q401C0; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0021545; P:cranial nerve development; IMP:UniProtKB.
DR   GO; GO:2000311; P:regulation of AMPA receptor activity; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR003377; Cornichon.
DR   InterPro; IPR033466; Cornichon_conserved.
DR   Pfam; PF03311; Cornichon; 2.
DR   SMART; SM01398; Cornichon; 1.
DR   PROSITE; PS01340; CORNICHON; 1.
PE   1: Evidence at protein level;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..160
FT                   /note="Protein cornichon homolog 2"
FT                   /id="PRO_0000408974"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..72
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   160 AA;  18781 MW;  466796F55100C14A CRC64;
     MAFTFAAFCY MLTLVLCASL IFFVIWHIIA FDELRTDFKN PIDQGNPARA RERLKNIERI
     CCLLRKLVVP EYCIHGLFCL MFLCAAEWVT LGLNLPLLLY HLWRYFHRPS DGSEGLFDAV
     SIMDADILGY CQKEAWCKLA FYLLSFFYYL YSMVYTLVSF