ID CAD18_BOVIN Reviewed; 790 AA.
AC Q08DJ5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 109.
DE RecName: Full=Cadherin-18;
DE Flags: Precursor;
GN Name=CDH18;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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; BC123714; AAI23715.1; -; mRNA.
DR RefSeq; NP_001070305.1; NM_001076837.1.
DR AlphaFoldDB; Q08DJ5; -.
DR SMR; Q08DJ5; -.
DR STRING; 9913.ENSBTAP00000031053; -.
DR GlyCosmos; Q08DJ5; 4 sites, No reported glycans.
DR PaxDb; 9913-ENSBTAP00000031053; -.
DR Ensembl; ENSBTAT00000031090.5; ENSBTAP00000031053.4; ENSBTAG00000037844.3.
DR GeneID; 512080; -.
DR KEGG; bta:512080; -.
DR CTD; 1016; -.
DR VEuPathDB; HostDB:ENSBTAG00000037844; -.
DR VGNC; VGNC:27097; CDH18.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000157512; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; Q08DJ5; -.
DR OMA; RTMQDVY; -.
DR OrthoDB; 3667774at2759; -.
DR TreeFam; TF329887; -.
DR Reactome; R-BTA-418990; Adherens junctions interactions.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000037844; Expressed in adenohypophysis and 23 other cell types or tissues.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
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: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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 5.
DR Gene3D; 2.60.40.60; Cadherins; 5.
DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 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_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027:SF106; CADHERIN-18; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 5.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; Cadherin-like; 5.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW Glycoprotein; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..53
FT /evidence="ECO:0000255"
FT /id="PRO_0000285120"
FT CHAIN 54..790
FT /note="Cadherin-18"
FT /id="PRO_0000285121"
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"
SQ SEQUENCE 790 AA; 87801 MW; 988992187363F637 CRC64;
MKITSTSCIC PVLVCLCFVQ RCYGTTHHGS IRGTRNQTKH 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 DGVGIFSIST DKETREGILS LKKPLNYEKK KSYTLNIEGA NTHLDFRFSH
LGPFKDATML KIIVGDVDEP PLFSMPSYVM EVYENAKIGT VVGTVLAQDP DSANSLVRYF
IDYNAEDDRF FNIDANTGTI KTTKVLDREE TPWYNITVAA SENDNPSLLS HVTVGIRVLD
VNDNPPELAR EYDIVVCENS KPGQVIHTIS ATDKDDFANG PRFNFFLDEH LSINPNFTLK
DNEDNTASIL TRRRRFSRTI QDVYYLPIMI SDGGIPSLSS SSTLTIRVCA CERDGRVRTC
HAEAFLSSAG LSTGALIAIL LCVVILLAIV VLFITLRRSK KEPLIISEED VRENVVTYDD
EGGGEEDTEA FDITALRNPS AAEELKYRRD IRPEVKLTPR HQTLSTLESI DVQEFIKQRL
AEADLDPSVP PYDSLQTYAY EGQRSEAGSI SSLDSATTQS DQDYQYLGDW GPEFKTLAEL
YGEIESERTT
//
