CAD17_RAT
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 03-AUG-2022, entry version 130.
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_008761743.1; XM_008763521.1.
DR RefSeq; XP_017448620.1; XM_017593131.1.
DR AlphaFoldDB; P55281; -.
DR SMR; P55281; -.
DR STRING; 10116.ENSRNOP00000021612; -.
DR GlyGen; P55281; 7 sites.
DR PaxDb; P55281; -.
DR PRIDE; P55281; -.
DR Ensembl; ENSRNOT00000021612; ENSRNOP00000021612; ENSRNOG00000015562.
DR GeneID; 117048; -.
DR KEGG; rno:117048; -.
DR UCSC; RGD:619748; rat.
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; RVHIVVQ; -.
DR OrthoDB; 190556at2759; -.
DR PhylomeDB; P55281; -.
DR TreeFam; TF316817; -.
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 tissues.
DR Genevisible; P55281; RN.
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; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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:RGD.
DR GO; GO:0005427; F:proton-dependent oligopeptide secondary active transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; ISO:RGD.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
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; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; 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:0035672; P:oligopeptide transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006857; P:oligopeptide transport; ISS:UniProtKB.
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 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; 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
