CAD18_HUMAN
ID CAD18_HUMAN Reviewed; 790 AA.
AC Q13634; A8K0I2; B4DHG6; Q8N5Z2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Cadherin-18;
DE AltName: Full=Cadherin-14;
DE Flags: Precursor;
GN Name=CDH18; Synonyms=CDH14;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9030594; DOI=10.1074/jbc.272.8.5236;
RA Shibata T., Shimoyama Y., Gotoh M., Hirohashi S.;
RT "Identification of human cadherin-14, a novel neurally specific type II
RT cadherin, by protein interaction cloning.";
RL J. Biol. Chem. 272:5236-5240(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13634-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13634-2; Sequence=VSP_042308;
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; U59325; AAB02933.1; -; mRNA.
DR EMBL; AK289547; BAF82236.1; -; mRNA.
DR EMBL; AK295087; BAG58128.1; -; mRNA.
DR EMBL; AC010490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC094103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC118463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471168; EAW68851.1; -; Genomic_DNA.
DR EMBL; BC031051; AAH31051.1; -; mRNA.
DR CCDS; CCDS3889.1; -. [Q13634-1]
DR CCDS; CCDS54835.1; -. [Q13634-2]
DR PIR; G02678; G02678.
DR RefSeq; NP_001161139.1; NM_001167667.1. [Q13634-2]
DR RefSeq; NP_001278885.1; NM_001291956.1. [Q13634-1]
DR RefSeq; NP_004925.1; NM_004934.3. [Q13634-1]
DR RefSeq; XP_005248285.1; XM_005248228.3. [Q13634-1]
DR RefSeq; XP_006714498.1; XM_006714435.3. [Q13634-1]
DR RefSeq; XP_016864413.1; XM_017008924.1. [Q13634-1]
DR RefSeq; XP_016864414.1; XM_017008925.1.
DR RefSeq; XP_016864415.1; XM_017008926.1. [Q13634-1]
DR RefSeq; XP_016864416.1; XM_017008927.1. [Q13634-1]
DR RefSeq; XP_016864417.1; XM_017008928.1. [Q13634-1]
DR RefSeq; XP_016864418.1; XM_017008929.1. [Q13634-1]
DR RefSeq; XP_016864419.1; XM_017008930.1. [Q13634-1]
DR RefSeq; XP_016864420.1; XM_017008931.1.
DR RefSeq; XP_016864421.1; XM_017008932.1.
DR RefSeq; XP_016864428.1; XM_017008939.1.
DR RefSeq; XP_016864429.1; XM_017008940.1.
DR RefSeq; XP_016864430.1; XM_017008941.1.
DR AlphaFoldDB; Q13634; -.
DR SMR; Q13634; -.
DR BioGRID; 107451; 5.
DR IntAct; Q13634; 1.
DR STRING; 9606.ENSP00000425093; -.
DR GlyGen; Q13634; 4 sites.
DR iPTMnet; Q13634; -.
DR PhosphoSitePlus; Q13634; -.
DR BioMuta; CDH18; -.
DR DMDM; 3023435; -.
DR MassIVE; Q13634; -.
DR PaxDb; Q13634; -.
DR PeptideAtlas; Q13634; -.
DR PRIDE; Q13634; -.
DR ProteomicsDB; 59625; -. [Q13634-1]
DR ProteomicsDB; 59626; -. [Q13634-2]
DR TopDownProteomics; Q13634-1; -. [Q13634-1]
DR Antibodypedia; 2730; 181 antibodies from 30 providers.
DR DNASU; 1016; -.
DR Ensembl; ENST00000274170.8; ENSP00000274170.3; ENSG00000145526.12. [Q13634-1]
DR Ensembl; ENST00000382275.6; ENSP00000371710.1; ENSG00000145526.12. [Q13634-1]
DR Ensembl; ENST00000502796.5; ENSP00000422138.1; ENSG00000145526.12. [Q13634-2]
DR Ensembl; ENST00000507958.5; ENSP00000425093.1; ENSG00000145526.12. [Q13634-1]
DR GeneID; 1016; -.
DR KEGG; hsa:1016; -.
DR MANE-Select; ENST00000382275.6; ENSP00000371710.1; NM_004934.5; NP_004925.1.
DR UCSC; uc003jgc.4; human. [Q13634-1]
DR CTD; 1016; -.
DR DisGeNET; 1016; -.
DR GeneCards; CDH18; -.
DR HGNC; HGNC:1757; CDH18.
DR HPA; ENSG00000145526; Tissue enriched (brain).
DR MIM; 603019; gene.
DR neXtProt; NX_Q13634; -.
DR OpenTargets; ENSG00000145526; -.
DR PharmGKB; PA26291; -.
DR VEuPathDB; HostDB:ENSG00000145526; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000157512; -.
DR HOGENOM; CLU_005284_3_0_1; -.
DR InParanoid; Q13634; -.
DR OMA; AEDDRCF; -.
DR OrthoDB; 240489at2759; -.
DR PhylomeDB; Q13634; -.
DR TreeFam; TF329887; -.
DR PathwayCommons; Q13634; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR SignaLink; Q13634; -.
DR SIGNOR; Q13634; -.
DR BioGRID-ORCS; 1016; 8 hits in 1068 CRISPR screens.
DR ChiTaRS; CDH18; human.
DR GenomeRNAi; 1016; -.
DR Pharos; Q13634; Tbio.
DR PRO; PR:Q13634; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q13634; protein.
DR Bgee; ENSG00000145526; Expressed in middle temporal gyrus and 137 other tissues.
DR ExpressionAtlas; Q13634; baseline and differential.
DR Genevisible; Q13634; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0034332; P:adherens junction organization; IBA:GO_Central.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..53
FT /evidence="ECO:0000255"
FT /id="PRO_0000003815"
FT CHAIN 54..790
FT /note="Cadherin-18"
FT /id="PRO_0000003816"
FT TOPO_DOM 54..608
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 609..636
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 637..790
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 54..159
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 160..268
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 269..383
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 384..486
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 487..608
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97326"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 544..790
FT /note="DNTASILTRRRRFSRTVQDVYYLPIMISDGGIPSLSSSSTLTIRVCACERDG
FT RVRTCHAEAFLSSAGLSTGALIAILLCVLILLAIVVLFITLRRSKKEPLIISEEDVREN
FT VVTYDDEGGGEEDTEAFDITALRNPSAAEELKYRRDIRPEVKLTPRHQTSSTLESIDVQ
FT EFIKQRLAEADLDPSVPPYDSLQTYAYEGQRSEAGSISSLDSATTQSDQDYHYLGDWGP
FT EFKKLAELYGEIESERTT -> AAAPSPSGFVHAREMGVCGPAMQKPSCPRLV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042308"
FT CONFLICT 226
FT /note="R -> G (in Ref. 5; AAH31051)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="P -> T (in Ref. 5; AAH31051)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="T -> I (in Ref. 5; AAH31051)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="E -> G (in Ref. 5; AAH31051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 88073 MW; 5C7BDEB229B6EDCA CRC64;
MKITSTSCIC PVLVCLCFVQ RCYGTAHHSS IKVMRNQTKH IEGETEVHHR PKRGWVWNQF
FVLEEHMGPD PQYVGKLHSN SDKGDGSVKY ILTGEGAGTI FIIDDTTGDI HSTKSLDREQ
KTHYVLHAQA IDRRTNKPLE PESEFIIKVQ DINDNAPKFT DGPYIVTVPE MSDMGTSVLQ
VTATDADDPT YGNSARVVYS ILQGQPYFSV DPKTGVIRTA LHNMDREARE HYSVVIQAKD
MAGQVGGLSG STTVNITLTD VNDNPPRFPQ KHYQLYVPES AQVGSAVGKI KANDADTGSN
ADMTYSIING DGMGIFSIST DKETREGILS LKKPLNYEKK KSYTLNIEGA NTHLDFRFSH
LGPFKDATML KIIVGDVDEP PLFSMPSYLM EVYENAKIGT VVGTVLAQDP DSTNSLVRYF
INYNVEDDRF FNIDANTGTI RTTKVLDREE TPWYNITVTA SEIDNPDLLS HVTVGIRVLD
VNDNPPELAR EYDIIVCENS KPGQVIHTIS ATDKDDFANG PRFNFFLDER LPVNPNFTLK
DNEDNTASIL TRRRRFSRTV QDVYYLPIMI SDGGIPSLSS SSTLTIRVCA CERDGRVRTC
HAEAFLSSAG LSTGALIAIL LCVLILLAIV VLFITLRRSK KEPLIISEED VRENVVTYDD
EGGGEEDTEA FDITALRNPS AAEELKYRRD IRPEVKLTPR HQTSSTLESI DVQEFIKQRL
AEADLDPSVP PYDSLQTYAY EGQRSEAGSI SSLDSATTQS DQDYHYLGDW GPEFKKLAEL
YGEIESERTT
