CAD17_MOUSE
ID CAD17_MOUSE Reviewed; 827 AA.
AC Q9R100;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cadherin-17;
DE AltName: Full=BILL-cadherin;
DE AltName: Full=Liver-intestine cadherin;
DE Short=LI-cadherin;
DE AltName: Full=P130;
DE Flags: Precursor;
GN Name=Cdh17;
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=Swiss Webster; TISSUE=Intestine;
RX PubMed=11376485; DOI=10.1002/dvdy.1146;
RA Angres B., Kim L., Jung R., Gessner R., Tauber R.;
RT "LI-cadherin gene expression during mouse intestinal development.";
RL Dev. Dyn. 221:182-193(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-33; 52-58; 74-81;
RP 117-123 AND 490-509, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Fetal liver;
RX PubMed=10906147; DOI=10.1074/jbc.m005901200;
RA Ohnishi K., Shimizu T., Karasuyama H., Melchers F.;
RT "The identification of a nonclassical cadherin expressed during B cell
RT development and its interaction with surrogate light chain.";
RL J. Biol. Chem. 275:31134-31144(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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).
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. LI-cadherin may have a role in the
CC morphological organization of liver and intestine.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highest expression is found in intestine with lower
CC expression in spleen, bone marrow, lung and testis. No expression
CC detected in liver, kidney, heart, brain or skeletal muscle. Expressed
CC in precursor B-cells and myeloid cells. {ECO:0000269|PubMed:10906147}.
CC -!- DEVELOPMENTAL STAGE: Expression increases in pro- and pre-B-I cells,
CC decreases in large and small pre-B-II cells, and increases again in
CC immature and mature B-cells. {ECO:0000269|PubMed:10906147}.
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; AF177669; AAD51125.1; -; mRNA.
DR EMBL; D87912; BAB03264.1; -; mRNA.
DR EMBL; BC042891; AAH42891.1; -; mRNA.
DR CCDS; CCDS17972.1; -.
DR RefSeq; NP_062727.1; NM_019753.4.
DR RefSeq; XP_006537646.1; XM_006537583.2.
DR RefSeq; XP_006537647.1; XM_006537584.3.
DR AlphaFoldDB; Q9R100; -.
DR SMR; Q9R100; -.
DR BioGRID; 198636; 4.
DR IntAct; Q9R100; 1.
DR STRING; 10090.ENSMUSP00000029871; -.
DR GlyGen; Q9R100; 7 sites.
DR iPTMnet; Q9R100; -.
DR PhosphoSitePlus; Q9R100; -.
DR MaxQB; Q9R100; -.
DR PaxDb; Q9R100; -.
DR PRIDE; Q9R100; -.
DR ProteomicsDB; 281742; -.
DR Antibodypedia; 12841; 445 antibodies from 41 providers.
DR DNASU; 12557; -.
DR Ensembl; ENSMUST00000029871; ENSMUSP00000029871; ENSMUSG00000028217.
DR GeneID; 12557; -.
DR KEGG; mmu:12557; -.
DR UCSC; uc008rzy.2; mouse.
DR CTD; 1015; -.
DR MGI; MGI:1095414; Cdh17.
DR VEuPathDB; HostDB:ENSMUSG00000028217; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000157655; -.
DR HOGENOM; CLU_016170_0_0_1; -.
DR InParanoid; Q9R100; -.
DR OMA; RVHIVVQ; -.
DR OrthoDB; 190556at2759; -.
DR PhylomeDB; Q9R100; -.
DR TreeFam; TF316817; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR BioGRID-ORCS; 12557; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9R100; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9R100; protein.
DR Bgee; ENSMUSG00000028217; Expressed in small intestine Peyer's patch and 42 other tissues.
DR ExpressionAtlas; Q9R100; baseline and differential.
DR Genevisible; Q9R100; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:CAFA.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0005427; F:proton-dependent oligopeptide secondary active transmembrane transporter activity; IDA:MGI.
DR GO; GO:0030183; P:B cell differentiation; IMP:UniProtKB.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:MGI.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0002314; P:germinal center B cell differentiation; IMP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0002315; P:marginal zone B cell differentiation; IMP:UniProtKB.
DR GO; GO:0006857; P:oligopeptide transport; IDA:MGI.
DR GO; GO:0033626; P:positive regulation of integrin activation by cell surface receptor linked signal transduction; ISO:MGI.
DR GO; GO:0048536; P:spleen development; IMP:UniProtKB.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR Pfam; PF00028; Cadherin; 5.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 7.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Direct protein sequencing;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:10906147"
FT CHAIN 26..827
FT /note="Cadherin-17"
FT /id="PRO_0000003813"
FT TOPO_DOM 26..786
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 808..827
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..127
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 128..243
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 244..339
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 340..448
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 449..565
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 566..666
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 667..776
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 827 AA; 91645 MW; CDCECEA5A76E2B58 CRC64;
MVSAQLHFLC LLTLYLTCGY GEEGKFSGPL KPMTFSIFEG QEPSQVIFQF KTNPPAVTFE
LTGETDGIFK IEKDGLLYHT RALDRETRAV HHLQLAALDS HGAIVDGPVP ITIEVKDIND
NRPTFLQSKY EGSVRQNSRP GKPFMYVNAT DLDDPATPNG QLFYQIVIQL PQINDVMYFQ
IDSKTGAISL TPEGSQELDP VKNPSYNLVV SVKDMGGQSE NSFSDTTYVD ISIRENIWKA
PEPVEIRENS TDPHPIKITQ VQWNDPGAQY SLVNKEKLSP FPFSIDQEGN IYVTQALDRE
EKNSHVFFAT AKDENGKPLA YPLEIYVKVI DINDNPPTCL SPVTVFEVQE NEPLGNSIGI
FEAHDMDEAN NINSILKYKL VDQTPKVPSD GLFLIGEYEG KVQLSKQSLK KQDSPQYNLS
IEVSDVDFKT LCYIQVNVID INDQIPIFET SNYGSKTLSE DTAIGSTILI IQATDADEPF
TGSSKILYKI VQGDTEGRLE VVTDPTTNAG YVKIKKPLDF ETQPVSSIVF QAENPEPLVK
GIEYNASSFA SFELIVTDVN EVPVFPQRIF QANVSEDAAV GSRVGNVTAR DPEGLTVSYS
LKGNMRGWLK IDSVTGEIFS AAPLDRETES VYRVQVVATE VGGSSLSSTA DFHLVLTDVN
DNPPRLAKDY TGLFFCHPLS APGSLIFEVT DDDQQSLRRP KFTFALGREG LQSDWEVSKI
NGTHARLSTR HTRFEEQVYN IPIRINDGGQ PPMEGTVFLP VTFCQCVEGS CFRPAGRQDG
IPTVGMAVGI LLTTFLVIGI ILAVVFIRMR KDKVENPQSP ENKPLRS
