ID I3J978_ORENI Unreviewed; 1166 AA.
AC I3J978;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Protocadherin 12 {ECO:0000313|Ensembl:ENSONIP00000005418.2};
GN Name=PCDH12 {ECO:0000313|Ensembl:ENSONIP00000005418.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000005418.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000005418.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_003447687.1; XM_003447639.4.
DR RefSeq; XP_005453287.1; XM_005453230.3.
DR AlphaFoldDB; I3J978; -.
DR STRING; 8128.ENSONIP00000005418; -.
DR Ensembl; ENSONIT00000005422.2; ENSONIP00000005418.2; ENSONIG00000004298.2.
DR GeneID; 100700015; -.
DR KEGG; onl:100700015; -.
DR CTD; 51294; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000160403; -.
DR HOGENOM; CLU_006480_1_2_1; -.
DR InParanoid; I3J978; -.
DR OMA; ALFMSIC; -.
DR OrthoDB; 4259465at2759; -.
DR TreeFam; TF352008; -.
DR Proteomes; UP000005207; Linkage group LG2.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
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; 6.
DR Gene3D; 2.60.40.60; Cadherins; 6.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF42; PROTOCADHERIN-12; 1.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF08266; Cadherin_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; Cadherin-like; 5.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1166
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025586235"
FT TRANSMEM 711..737
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..129
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 130..238
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 239..346
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 352..457
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 458..562
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 611..705
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 751..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1142..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1017
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 127696 MW; AED821982ACBDB67 CRC64;
MLLALLLVVS LCSKTLSSHC SSTTIQYQVS EEQPAGTRVG CLADDLRQRD EGGSLEDFQV
VEQGKALPFS VTTRDGVVST QGRLDREELC RGTDLCEVAF SVLYRKRGAV KCLRVHVKVM
DLNDHSPSFP NTLQEVEISE TASLGKRILL DWAVDPDAGS NSLQNYSLSV NQHFDLDVTV
GPGGTKQAEL VVVQELDREI QASFDLTLVA WDKGNPPRSG STLVRVSIQD SNDNSPTFED
SNPTVSLPED TALGTTVIKL KATDPDQGAN GEVEYSFSKH THPEVQRLFY VDPQTGEVSI
RAPLDYEAQS SYEVIVQASD RGPNAIPSYC RLHIKLIDIN DNAPRIRLTW TPASSQVITV
LEGAPEDTLL AVVTVSDADS GRNGNVTAQI QQGSGPFRLK KMHGNDYMIV TSGSLDREKV
MQYNITLFAR DSGNPLLSCV EHLPVYVLDE NDNAPVFSTP IYRASFKENN MTGYHILKVE
AHDEDLELSG KVSYSIAEEA KTQPFSIHPK TGVISVQQPL DYEAFKNYSF IVEAVDHGHP
PLTSTARVHI DIEDVNDNFP VIKEPKPRKG VASLSVPVDA YRGEIVTEMG NAIKEEATNV
ATDHSVREGL GFLASTIKAE DQDTGLNGKL QYLITDGNLS ELFWLNNTSG QLFVNTTNAT
ELIGKTFKVD ITVSDMGTPR LATKATLEVT FINLKDHLKN SSPGNRGQLS FTMMMAICLG
ATCLLLLLAI ALVTTFCRPE KRDNRAYNCR QAESTYTRHP RRPQKNIRKS DIQLIPVIRG
RKEDLPEDDG EAQPLTPPPV SDDQQIESHY SLMPSVMNAS FHSQGYLEED VTQPNTHHCR
TLRKPGNIEL DGTLPSSPAT SYRTLRKSRN TSSSSSVSHS STLKRQKNSE GEETVSQYSS
ASVATLRRPK TSDGHGARDA EHRQILRNLV RLSMAAFGDS IELSSASPEV QQISQLLSLL
HQGQLQPRPN FRGNKYSHRN GRYGGQDCSD WQSTKDSGHG ESEAGDVDWE PGRDSPIDPQ
LEEGLSNLLN NPDDVFSEVS DPSWMARLSL PLTSNYHDNV FVPNGPPSPE SETLPRDCLE
SSSFSTFGKT PEKDGSLGGA LLSEVSTLFE MLMTQKADAH PGPRPDVLYR LSAAYRRSLG
LDGGAAGNAA KNSARSGPSA PSGLCQ
//
