CEA16_MOUSE
ID CEA16_MOUSE Reviewed; 426 AA.
AC E9QA28; B2RUD6;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Carcinoembryonic antigen-related cell adhesion molecule 16;
DE Flags: Precursor;
GN Name=Ceacam16;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, MUTAGENESIS OF THR-142, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21368133; DOI=10.1073/pnas.1005842108;
RA Zheng J., Miller K.K., Yang T., Hildebrand M.S., Shearer A.E., DeLuca A.P.,
RA Scheetz T.E., Drummond J., Scherer S.E., Legan P.K., Goodyear R.J.,
RA Richardson G.P., Cheatham M.A., Smith R.J., Dallos P.;
RT "Carcinoembryonic antigen-related cell adhesion molecule 16 interacts with
RT alpha-tectorin and is mutated in autosomal dominant hearing loss (DFNA4).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4218-4223(2011).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH TECTA AND TECTB.
RX PubMed=25080593; DOI=10.1523/jneurosci.1256-14.2014;
RA Cheatham M.A., Goodyear R.J., Homma K., Legan P.K., Korchagina J.,
RA Naskar S., Siegel J.H., Dallos P., Zheng J., Richardson G.P.;
RT "Loss of the tectorial membrane protein CEACAM16 enhances spontaneous,
RT stimulus-frequency, and transiently evoked otoacoustic emissions.";
RL J. Neurosci. 34:10325-10338(2014).
CC -!- FUNCTION: Required for proper hearing, plays a role in maintaining the
CC integrity of the tectorial membrane. {ECO:0000269|PubMed:25080593}.
CC -!- SUBUNIT: Homooligomer; can for homodimers and homotetramers (By
CC similarity). Interacts with TECTA and TECTB (PubMed:25080593).
CC {ECO:0000250|UniProtKB:Q2WEN9, ECO:0000269|PubMed:25080593}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21368133}.
CC Note=Localizes at the tip of cochlear outer hair cells and to the
CC tectorial membrane. {ECO:0000269|PubMed:21368133}.
CC -!- TISSUE SPECIFICITY: Expressed in cochlear outer hair cells (OHC).
CC {ECO:0000269|PubMed:21368133}.
CC -!- DEVELOPMENTAL STAGE: Abundantly expressed in cochleae from embryonic
CC day 17 to postnatal day 42. {ECO:0000269|PubMed:21368133}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice show loss of striated-sheet matrix
CC and Hensen's stripe, a prominent feature in the basal two-thirds of the
CC tectorial membrane. They have enhanced spontaneous, stimulus-frequency,
CC and transiently evoked otoacoustic emissions.
CC {ECO:0000269|PubMed:25080593}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
CC {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; AC149085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC141087; AAI41088.1; -; mRNA.
DR CCDS; CCDS39805.1; -.
DR RefSeq; NP_001028591.2; NM_001033419.2.
DR RefSeq; XP_006540172.1; XM_006540109.2.
DR RefSeq; XP_006540173.1; XM_006540110.2.
DR RefSeq; XP_011248907.1; XM_011250605.2.
DR AlphaFoldDB; E9QA28; -.
DR STRING; 10090.ENSMUSP00000014830; -.
DR GlyGen; E9QA28; 2 sites.
DR iPTMnet; E9QA28; -.
DR PhosphoSitePlus; E9QA28; -.
DR PaxDb; E9QA28; -.
DR PRIDE; E9QA28; -.
DR Antibodypedia; 31203; 131 antibodies from 26 providers.
DR Ensembl; ENSMUST00000014830; ENSMUSP00000014830; ENSMUSG00000014686.
DR GeneID; 330483; -.
DR KEGG; mmu:330483; -.
DR UCSC; uc009fnm.1; mouse.
DR CTD; 388551; -.
DR MGI; MGI:2685615; Ceacam16.
DR VEuPathDB; HostDB:ENSMUSG00000014686; -.
DR eggNOG; ENOG502S42Z; Eukaryota.
DR GeneTree; ENSGT00960000186634; -.
DR HOGENOM; CLU_024555_2_0_1; -.
DR InParanoid; E9QA28; -.
DR OMA; GQDHVNI; -.
DR OrthoDB; 998214at2759; -.
DR PhylomeDB; E9QA28; -.
DR TreeFam; TF336859; -.
DR BioGRID-ORCS; 330483; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Ceacam16; mouse.
DR PRO; PR:E9QA28; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; E9QA28; protein.
DR Bgee; ENSMUSG00000014686; Expressed in internal ear and 24 other tissues.
DR ExpressionAtlas; E9QA28; baseline and differential.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0032426; C:stereocilium tip; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..426
FT /note="Carcinoembryonic antigen-related cell adhesion
FT molecule 16"
FT /id="PRO_0000417874"
FT DOMAIN 134..219
FT /note="Ig-like C2-type 1"
FT DOMAIN 224..310
FT /note="Ig-like C2-type 2"
FT REGION 77..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 155..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 253..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 142
FT /note="T->P: Does not affect the interaction with TECTA nor
FT subcellular localization."
FT /evidence="ECO:0000269|PubMed:21368133"
FT CONFLICT 133
FT /note="A -> T (in Ref. 2; AAI41088)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="M -> T (in Ref. 2; AAI41088)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 46352 MW; B2A348370AB0AB46 CRC64;
MKMPLTWYSW FLLSAWILNT GAEISITPEP AQPAEGDNVT LVVHGLSGEL LAYNWYAGPT
LSLTFLVASY IVSTGDETPG PAHTGREAVR PDGSLDIHGA LPGHTGTYIL QTLNRQFQTE
VGYGHMQVYE ILAPPTVMAN DTALVERRDT LRLVCSSPSP AEVRWFFNGD ALPVAVRLGM
SPDGRMLTRH GVRREEAGAY QCEVWNPVSV SRSEPLNLTV YFGPERVAIL QDSTTRTGCT
IKVDFNMSLT LWCVARSCPE PEYVWAFNGK ALKNGQDHLN ISSMTAAHEG TYTCIAKNSK
TLLSGSASVV VKLSAAAVAM MIVPVPTKPT EGQDVTLTVQ GYPKDLLVYA WYRGPASEPN
RLLSQLPSGN WIAGPAHTGR EVGFANCSLL VQKLNLTDAG RYTLKTVTLQ GKTDTLEVEL
QVAPLE
