ID A0A2K5ZBA0_MANLE Unreviewed; 790 AA.
AC A0A2K5ZBA0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cadherin 18 {ECO:0000313|Ensembl:ENSMLEP00000025077.1};
GN Name=CDH18 {ECO:0000313|Ensembl:ENSMLEP00000025077.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000025077.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000025077.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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DR RefSeq; XP_011840370.1; XM_011984980.1.
DR RefSeq; XP_011840371.1; XM_011984981.1.
DR AlphaFoldDB; A0A2K5ZBA0; -.
DR STRING; 9568.ENSMLEP00000025077; -.
DR Ensembl; ENSMLET00000048605.1; ENSMLEP00000025077.1; ENSMLEG00000036705.1.
DR GeneID; 105543182; -.
DR KEGG; mleu:105543182; -.
DR CTD; 1016; -.
DR GeneTree; ENSGT00940000157512; -.
DR OMA; RTMQDVY; -.
DR OrthoDB; 3667774at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
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; 2.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003318};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..790
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014462461"
FT TRANSMEM 615..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..159
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 160..268
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 269..383
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 384..488
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 488..605
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
SQ SEQUENCE 790 AA; 87936 MW; A7DAD5E920B3B52C CRC64;
MKITSTSCIC PVLVCLCFVQ RCYGTAHHSS IKVTRNQTKH 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 LQKPLNYEKK KSYTLNIEGA NTHLDFRFSH
LGPFKDATML KIIVGDVDEP PLFSMPSYVM EVYENAKIGT VVGTVLAQDP DSANSLVRYF
INYNAEDDRF FNIDANTGTI KTTKVLDREE TPWYNITVTA SENDNPDLLS HVTVGIRVLD
VNDNPPELAR EYDIVVCENS KPGQVIHTIS ATDKDDFANG PRFNFFLDEH LPVNPNFTLK
DNEDNTASIL TRRRRFSRTV QDVYYLPIMI SDGGIPSLSS SSTLTIRVCA CERDGRVRTC
HAEAFLSSAG LSTGALIAIL LCVLILLAIV VIFITLRRSK KEPLIISEED VRENVVTYDD
EGGGEEDTEA FDITALRNPS AAEELKYRRD IRPEVKLTPR HQTLSTLESI DVQEFIKQRL
AEADLDPSVP PYDSLQTYAY EGQRSEAGSI SSLDSATTQS DQDYHYLGDW GPEFKKLAEL
YGEIESERTT
//