ID   CAD17_RAT               Reviewed;         827 AA.
AC   P55281;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   10-JUN-2026, entry version 145.
DE   RecName: Full=Cadherin-17;
DE   AltName: Full=Liver-intestine cadherin;
DE            Short=LI-cadherin;
DE   Flags: Precursor;
GN   Name=Cdh17;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8207063; DOI=10.1083/jcb.125.6.1353;
RA   Berndorff D., Gessner R., Kreft B., Schnoy N., Lajous-Petter A.-M.,
RA   Loch N., Reutter W., Hortsch M., Tauber R.;
RT   "Liver-intestine cadherin: molecular cloning and characterization of a
RT   novel Ca(2+)-dependent cell adhesion molecule expressed in liver and
RT   intestine.";
RL   J. Cell Biol. 125:1353-1369(1994).
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; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Liver and intestine.
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; X78997; CAA55631.1; -; mRNA.
DR   PIR; A53954; A53954.
DR   RefSeq; NP_446429.1; NM_053977.2.
DR   RefSeq; XP_063143150.1; XM_063287080.1.
DR   RefSeq; XP_063143151.1; XM_063287081.1.
DR   RefSeq; XP_063143152.1; XM_063287082.1.
DR   AlphaFoldDB; P55281; -.
DR   SMR; P55281; -.
DR   FunCoup; P55281; 35.
DR   STRING; 10116.ENSRNOP00000021612; -.
DR   GlyCosmos; P55281; 7 sites, No reported glycans.
DR   GlyGen; P55281; 7 sites.
DR   PhosphoSitePlus; P55281; -.
DR   PaxDb; 10116-ENSRNOP00000021612; -.
DR   Ensembl; ENSRNOT00000021612.6; ENSRNOP00000021612.2; ENSRNOG00000015562.6.
DR   Ensembl; ENSRNOT00055035370; ENSRNOP00055028672; ENSRNOG00055020678.
DR   Ensembl; ENSRNOT00060029524; ENSRNOP00060023742; ENSRNOG00060017185.
DR   Ensembl; ENSRNOT00065025593; ENSRNOP00065020102; ENSRNOG00065015406.
DR   GeneID; 117048; -.
DR   KEGG; rno:117048; -.
DR   UCSC; RGD:619748; rat.
DR   AGR; RGD:619748; -.
DR   CTD; 1015; -.
DR   RGD; 619748; Cdh17.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000157655; -.
DR   HOGENOM; CLU_016170_0_0_1; -.
DR   InParanoid; P55281; -.
DR   OMA; DVNNEMP; -.
DR   PhylomeDB; P55281; -.
DR   Reactome; R-RNO-418990; Adherens junctions interactions.
DR   PRO; PR:P55281; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000015562; Expressed in jejunum and 17 other cell types or tissues.
DR   ExpressionAtlas; P55281; baseline and differential.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0030054; C:cell junction; ISO:RGD.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR   GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005178; F:integrin binding; ISO:RGD.
DR   GO; GO:0005427; F:proton-dependent oligopeptide secondary active transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR   GO; GO:0030183; P:B cell differentiation; ISO:RGD.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IBA:GO_Central.
DR   GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR   GO; GO:0002314; P:germinal center B cell differentiation; ISO:RGD.
DR   GO; GO:0007156; P:homophilic cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0002315; P:marginal zone B cell differentiation; ISO:RGD.
DR   GO; GO:0006857; P:oligopeptide transport; ISO:RGD.
DR   GO; GO:0033626; P:positive regulation of integrin activation by cell surface receptor linked signal transduction; ISO:RGD.
DR   GO; GO:0048536; P:spleen development; ISO:RGD.
DR   CDD; cd11304; Cadherin_repeat; 6.
DR   FunFam; 2.60.40.60:FF:000151; Cadherin 17; 1.
DR   FunFam; 2.60.40.60:FF:000152; Cadherin 17; 1.
DR   FunFam; 2.60.40.60:FF:000163; Cadherin 17; 1.
DR   FunFam; 2.60.40.60:FF:000169; Cadherin 17; 1.
DR   FunFam; 2.60.40.60:FF:000183; Cadherin 17; 1.
DR   FunFam; 2.60.40.60:FF:000188; Cadherin 17; 1.
DR   FunFam; 2.60.40.60:FF:000212; Cadherin 17; 1.
DR   Gene3D; 2.60.40.60; Cadherins; 7.
DR   InterPro; IPR039808; Cadherin.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   PANTHER; PTHR24027:SF419; CADHERIN-17; 1.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   Pfam; PF00028; Cadherin; 5.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; Cadherin-like; 7.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW   Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..827
FT                   /note="Cadherin-17"
FT                   /id="PRO_0000003814"
FT   TOPO_DOM        22..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        183
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        721
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   827 AA;  91863 MW;  E1A0B03646562C01 CRC64;
     MVSAQLHFLC LLTLYLTGAY GQEGKFSGPL KPMTFSIFEG QEPSQIIFQF KANPPAVTFE
     LTGETDGIFK IEKDGLLYHT RVLDRETRAV HHLQLAALDS QGAIVDGPVP IIIEVKDIND
     NRPTFLQTKY EGSVRQNSRP GKPFMYVNAT DLDDPATPNG QLFYQIVIQL PKINNVMYFQ
     IDNKTGAISL TPEGSQVLDP IKNPYYNLVV SVKDMGGQNE NSFSDTTSVD ITVRENIWKA
     PEPVEIRENL TDPHPIKITQ VQWNDPGAHY SLINKEKLPQ FPFSIDQEGN IYVTQPLDRE
     EKDSHVFFAT AKDENGKPLA YPLEIRVKVI DINDNPPTCL SQVTVFEVQE NEVLGSSIGI
     FAAHDMDEAN NINSILKYRL VDQTPKVPSD ELFLIDEYGG KVQLGKRSLK KQDSPQYNLT
     VEVSDIDFKT LCSLQVNVID INDQIPIFER SDYGSKTLSE DTAIGSTILI IQATDDDEPF
     TGSSKILYKI VQGDTEGRLE VVTDPMTNTG YVKIRKPLDF ETEPVTSIVF KAENPEPLVN
     GIEYNASSFA SFELTVTDVN EVPVFPQQIF QANVSEDTAI GTKVGTVTAR DPEGLTVSYS
     LKDNKRGWLK IDSVTGDIFS TAPLDRETES VYRVQVVATE VGGSSLSSTA YFHLVLMDVN
     DNPPRLAKDY TGLFFCHPLS APGSLIFEAT DDDQQSVRRP KFTFALGRES LQSDWEVSKI
     NGTHARLSTK HTRFEEQVYD IPILINDGGQ PPMEGIVSLS VTFCQCVDGS CFRPAGNQVG
     IPTVGMAVGI LLTTFLVIGI ILAVVFIRMR KDKVEDPQSP ENKPLRS
//