CAD17_HUMAN
ID CAD17_HUMAN Reviewed; 832 AA.
AC Q12864; Q15336; Q2M2E0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Cadherin-17;
DE AltName: Full=Intestinal peptide-associated transporter HPT-1;
DE AltName: Full=Liver-intestine cadherin;
DE Short=LI-cadherin;
DE Flags: Precursor;
GN Name=CDH17;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANTS
RP GLU-115 AND ASP-734.
RC TISSUE=Colon adenocarcinoma;
RX PubMed=8153632; DOI=10.1126/science.8153632;
RA Dantzig A.H., Hoskins J., Tabas L.B., Bright S., Shepard R.L.,
RA Jenkins I.L., Duckworth D.C., Sportsman J.R., MacKensen D.,
RA Rosteck P.R. Jr., Skatrud P.L.;
RT "Association of intestinal peptide transport with a protein related to the
RT cadherin superfamily.";
RL Science 264:430-433(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-446.
RA Boettinger A., Kreft B., Fieger C., Dlouhy B., Berndorff D., Goessner R.,
RA Tauber R.;
RT "Molecular cloning of human LI-cadherin: evidence for a novel type of
RT cadherin within the cadherin superfamily.";
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-115 AND ASP-734.
RC TISSUE=Cerebellum;
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. Involved in
CC intestinal peptide transport. {ECO:0000269|PubMed:8153632}.
CC -!- INTERACTION:
CC Q12864; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12278850, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the gastrointestinal tract and
CC pancreatic duct. Not detected in kidney, lung, liver, brain, adrenal
CC gland and skin. {ECO:0000269|PubMed:8153632}.
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}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CDH17ID40020ch8q22.html";
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DR EMBL; U07969; AAA19021.1; -; mRNA.
DR EMBL; X83228; CAA58231.1; -; mRNA.
DR EMBL; AP003351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC112013; AAI12014.1; -; mRNA.
DR EMBL; BC113464; AAI13465.1; -; mRNA.
DR CCDS; CCDS6260.1; -.
DR PIR; S55396; S55396.
DR RefSeq; NP_001138135.1; NM_001144663.1.
DR RefSeq; NP_004054.3; NM_004063.3.
DR PDB; 6ULM; X-ray; 2.15 A; A/B=23-241.
DR PDB; 7CYM; X-ray; 2.70 A; A/B=23-441.
DR PDB; 7EV1; X-ray; 1.38 A; A/B=29-236.
DR PDBsum; 6ULM; -.
DR PDBsum; 7CYM; -.
DR PDBsum; 7EV1; -.
DR AlphaFoldDB; Q12864; -.
DR SMR; Q12864; -.
DR BioGRID; 107450; 8.
DR IntAct; Q12864; 3.
DR STRING; 9606.ENSP00000027335; -.
DR GlyGen; Q12864; 9 sites.
DR iPTMnet; Q12864; -.
DR PhosphoSitePlus; Q12864; -.
DR BioMuta; CDH17; -.
DR DMDM; 308153624; -.
DR jPOST; Q12864; -.
DR MassIVE; Q12864; -.
DR MaxQB; Q12864; -.
DR PaxDb; Q12864; -.
DR PeptideAtlas; Q12864; -.
DR PRIDE; Q12864; -.
DR ProteomicsDB; 58991; -.
DR ABCD; Q12864; 14 sequenced antibodies.
DR Antibodypedia; 12841; 445 antibodies from 41 providers.
DR DNASU; 1015; -.
DR Ensembl; ENST00000027335.8; ENSP00000027335.3; ENSG00000079112.10.
DR Ensembl; ENST00000450165.6; ENSP00000401468.2; ENSG00000079112.10.
DR GeneID; 1015; -.
DR KEGG; hsa:1015; -.
DR MANE-Select; ENST00000027335.8; ENSP00000027335.3; NM_004063.4; NP_004054.3.
DR UCSC; uc003ygh.3; human.
DR CTD; 1015; -.
DR DisGeNET; 1015; -.
DR GeneCards; CDH17; -.
DR HGNC; HGNC:1756; CDH17.
DR HPA; ENSG00000079112; Tissue enriched (intestine).
DR MIM; 603017; gene.
DR neXtProt; NX_Q12864; -.
DR OpenTargets; ENSG00000079112; -.
DR PharmGKB; PA26290; -.
DR VEuPathDB; HostDB:ENSG00000079112; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000157655; -.
DR HOGENOM; CLU_016170_0_0_1; -.
DR InParanoid; Q12864; -.
DR OMA; RVHIVVQ; -.
DR OrthoDB; 190556at2759; -.
DR PhylomeDB; Q12864; -.
DR TreeFam; TF316817; -.
DR PathwayCommons; Q12864; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR SignaLink; Q12864; -.
DR SIGNOR; Q12864; -.
DR BioGRID-ORCS; 1015; 8 hits in 1072 CRISPR screens.
DR ChiTaRS; CDH17; human.
DR GeneWiki; CDH17; -.
DR GenomeRNAi; 1015; -.
DR Pharos; Q12864; Tbio.
DR PRO; PR:Q12864; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q12864; protein.
DR Bgee; ENSG00000079112; Expressed in colonic mucosa and 110 other tissues.
DR ExpressionAtlas; Q12864; baseline and differential.
DR Genevisible; Q12864; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; IPI:UniProtKB.
DR GO; GO:0005427; F:proton-dependent oligopeptide secondary active transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
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; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0002315; P:marginal zone B cell differentiation; IEA:Ensembl.
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; IMP:UniProtKB.
DR GO; GO:0048536; P:spleen development; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell membrane; Glycoprotein;
KW Membrane; Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..832
FT /note="Cadherin-17"
FT /id="PRO_0000003812"
FT TOPO_DOM 23..787
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 788..808
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 809..832
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..128
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 129..244
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 245..340
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 341..449
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 450..566
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 567..667
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 668..777
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 115
FT /note="K -> E (in dbSNP:rs2243518)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8153632"
FT /id="VAR_055567"
FT VARIANT 446
FT /note="I -> T (in dbSNP:rs1131829)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_031694"
FT VARIANT 734
FT /note="E -> D (in dbSNP:rs1051623)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8153632"
FT /id="VAR_031695"
FT VARIANT 739
FT /note="E -> A (in dbSNP:rs1051624)"
FT /id="VAR_031696"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:6ULM"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:7EV1"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:7EV1"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 105..117
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6ULM"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:7EV1"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:7EV1"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:7EV1"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 206..215
FT /evidence="ECO:0007829|PDB:7EV1"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:6ULM"
FT STRAND 225..235
FT /evidence="ECO:0007829|PDB:7EV1"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:7CYM"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:7CYM"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:7CYM"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:7CYM"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:7CYM"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:7CYM"
FT STRAND 304..313
FT /evidence="ECO:0007829|PDB:7CYM"
FT STRAND 324..331
FT /evidence="ECO:0007829|PDB:7CYM"
FT STRAND 341..350
FT /evidence="ECO:0007829|PDB:7CYM"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:7CYM"
FT TURN 373..375
FT /evidence="ECO:0007829|PDB:7CYM"
FT STRAND 378..386
FT /evidence="ECO:0007829|PDB:7CYM"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:7CYM"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:7CYM"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:7CYM"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:7CYM"
FT STRAND 416..425
FT /evidence="ECO:0007829|PDB:7CYM"
FT STRAND 430..440
FT /evidence="ECO:0007829|PDB:7CYM"
SQ SEQUENCE 832 AA; 92219 MW; 2707547DD2DB4202 CRC64;
MILQAHLHSL CLLMLYLATG YGQEGKFSGP LKPMTFSIYE GQEPSQIIFQ FKANPPAVTF
ELTGETDNIF VIEREGLLYY NRALDRETRS THNLQVAALD ANGIIVEGPV PITIKVKDIN
DNRPTFLQSK YEGSVRQNSR PGKPFLYVNA TDLDDPATPN GQLYYQIVIQ LPMINNVMYF
QINNKTGAIS LTREGSQELN PAKNPSYNLV ISVKDMGGQS ENSFSDTTSV DIIVTENIWK
APKPVEMVEN STDPHPIKIT QVRWNDPGAQ YSLVDKEKLP RFPFSIDQEG DIYVTQPLDR
EEKDAYVFYA VAKDEYGKPL SYPLEIHVKV KDINDNPPTC PSPVTVFEVQ ENERLGNSIG
TLTAHDRDEE NTANSFLNYR IVEQTPKLPM DGLFLIQTYA GMLQLAKQSL KKQDTPQYNL
TIEVSDKDFK TLCFVQINVI DINDQIPIFE KSDYGNLTLA EDTNIGSTIL TIQATDADEP
FTGSSKILYH IIKGDSEGRL GVDTDPHTNT GYVIIKKPLD FETAAVSNIV FKAENPEPLV
FGVKYNASSF AKFTLIVTDV NEAPQFSQHV FQAKVSEDVA IGTKVGNVTA KDPEGLDISY
SLRGDTRGWL KIDHVTGEIF SVAPLDREAG SPYRVQVVAT EVGGSSLSSV SEFHLILMDV
NDNPPRLAKD YTGLFFCHPL SAPGSLIFEA TDDDQHLFRG PHFTFSLGSG SLQNDWEVSK
INGTHARLST RHTEFEEREY VVLIRINDGG RPPLEGIVSL PVTFCSCVEG SCFRPAGHQT
GIPTVGMAVG ILLTTLLVIG IILAVVFIRI KKDKGKDNVE SAQASEVKPL RS
