CAD16_MOUSE
ID CAD16_MOUSE Reviewed; 830 AA.
AC O88338; Q9JLZ5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cadherin-16;
DE AltName: Full=Kidney-specific cadherin;
DE Short=Ksp-cadherin;
DE Flags: Precursor;
GN Name=Cdh16;
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 [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=9721215; DOI=10.1006/geno.1998.5402;
RA Thomson R.B., Ward D.C., Quaggin S.E., Igarashi P., Muckler Z.E.,
RA Aronson P.S.;
RT "cDNA cloning and chromosomal localization of the human and mouse isoforms
RT of Ksp-cadherin.";
RL Genomics 51:445-451(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE OF 1-25.
RC STRAIN=129/Sv;
RX PubMed=10516284; DOI=10.1152/ajprenal.1999.277.4.f587;
RA Whyte D.A., Li C., Thomson R.B., Nix S.L., Zanjani R., Karp S.L.,
RA Aronson P.S., Igarashi P.;
RT "Ksp-cadherin gene promoter. I. Characterization and renal epithelial cell-
RT specific activity.";
RL Am. J. Physiol. 277:F587-F598(1999).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-823, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells; cadherins may thus contribute to the sorting of
CC heterogeneous cell types.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Kidney specific.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. {ECO:0000250}.
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DR EMBL; AF016271; AAC34254.1; -; mRNA.
DR EMBL; BC015251; AAH15251.1; -; mRNA.
DR EMBL; AF118228; AAF28836.1; -; Genomic_DNA.
DR CCDS; CCDS22583.1; -.
DR RefSeq; NP_031689.1; NM_007663.3.
DR AlphaFoldDB; O88338; -.
DR SMR; O88338; -.
DR STRING; 10090.ENSMUSP00000129663; -.
DR GlyGen; O88338; 3 sites.
DR iPTMnet; O88338; -.
DR PhosphoSitePlus; O88338; -.
DR jPOST; O88338; -.
DR PaxDb; O88338; -.
DR PeptideAtlas; O88338; -.
DR PRIDE; O88338; -.
DR ProteomicsDB; 265494; -.
DR Antibodypedia; 29333; 601 antibodies from 31 providers.
DR DNASU; 12556; -.
DR Ensembl; ENSMUST00000211903; ENSMUSP00000148478; ENSMUSG00000031881.
DR GeneID; 12556; -.
DR KEGG; mmu:12556; -.
DR UCSC; uc009nax.2; mouse.
DR CTD; 1014; -.
DR MGI; MGI:106671; Cdh16.
DR VEuPathDB; HostDB:ENSMUSG00000031881; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000161650; -.
DR HOGENOM; CLU_016170_1_0_1; -.
DR InParanoid; O88338; -.
DR OMA; QHEYGPF; -.
DR OrthoDB; 190556at2759; -.
DR PhylomeDB; O88338; -.
DR TreeFam; TF316817; -.
DR BioGRID-ORCS; 12556; 4 hits in 72 CRISPR screens.
DR PRO; PR:O88338; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O88338; protein.
DR Bgee; ENSMUSG00000031881; Expressed in adult mammalian kidney and 65 other tissues.
DR ExpressionAtlas; O88338; baseline and differential.
DR Genevisible; O88338; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR InterPro; IPR030721; Cadherin-16.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR PANTHER; PTHR24028:SF1; PTHR24028:SF1; 1.
DR Pfam; PF00028; Cadherin; 4.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 1.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..830
FT /note="Cadherin-16"
FT /id="PRO_0000003810"
FT TOPO_DOM 22..788
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 789..809
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 810..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..128
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 133..237
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 244..338
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 343..451
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 457..566
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 571..667
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 668..788
FT /note="Ectodomain G"
FT MOD_RES 823
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 830 AA; 89860 MW; 5EB1F06B5B7C2F25 CRC64;
MISARPWLLY LSVIQAFTTE AQPAESLHTE VPENYGGNFP FYILKLPLPL GRDEGHIVLS
GDSNTADQNT FAVDTDSGFL VATRTLDREE KAEYQLQVTL ESEDGRILWG PQLVTVHVKD
ENDQVPQFSQ AIYRAQLSQG TRPGVPFLFL EASDGDAPGT ANSDLRFHIL SQSPPQPLPD
MFQLDPHLGA LALSPSGSTS LDHALEETYQ LLVQVKDMGD QPSGHQAIAT VEISIVENSW
APLEPVHLAE NLKVVYPHSI AQVHWSGGDV HYQLESQPPG PFDVDTEGML HVTMELDREA
QAEYQLQVRA QNSHGEDYAE PLELQVVVMD ENDNAPVCSP HDPTVNIPEL SPPGTEIARL
SAEDLDAPGS PNSHIVYQLL SPEPEEGAEN KAFELDPTSG SVTLGTAPLH AGQSILLQVL
AVDLAGSESG LSSTCEVTVM VTDVNNHAPE FINSQIGPVT LPEDVKPGAL VATLMATDAD
LEPAFRLMDF AIEEGDPEGI FDLSWEPDSD HVQLRLRKNL SYEAAPDHKV VVVVSNIEEL
VGPGPGPAAT ATVTILVERV VAPLKLDQES YETSIPVSTP AGSLLLTIQP SDPMSRTLRF
SLVNDSEGWL CIKEVSGEVH TAQSLQGAQP GDTYTVLVEA QDTDKPGLST SATVVIHFLK
ASPVPALTLS AGPSRHLCTP RQDYGVVVSG VSEDPDLANR NGPYSFALGP NPTVQRDWRL
QPLNDSHAYL TLALHWVEPG EYMVPVVVHH DTHMWQLQVK VIVCRCNVEG QCMRKVGRMK
GMPTKLSAVG VLLGTLAAIG FILILVFTHL ALARKDLDQP ADSVPLKAAV
