ID H2T9F6_TAKRU Unreviewed; 1169 AA.
AC H2T9F6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Protocadherin 12 {ECO:0000313|Ensembl:ENSTRUP00000021296.3};
GN Name=PCDH12 {ECO:0000313|Ensembl:ENSTRUP00000021296.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000021296.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000021296.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000021296.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; H2T9F6; -.
DR STRING; 31033.ENSTRUP00000021296; -.
DR Ensembl; ENSTRUT00000021384.3; ENSTRUP00000021296.3; ENSTRUG00000008500.3.
DR GeneTree; ENSGT00940000160403; -.
DR InParanoid; H2T9F6; -.
DR OMA; FHVDSQT; -.
DR Proteomes; UP000005226; Chromosome 14.
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; 5.
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:UP000005226};
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..1169
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025644144"
FT TRANSMEM 712..738
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 359..457
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 458..565
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 597..706
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 749..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1169 AA; 127069 MW; 85AEE3E0753FDBA4 CRC64;
MLLLLLLLSD LCCDVRASES TSVTLQYRVW EEQPSGTRVG CLVDDLRQRD EGGPFEDFQV
VEHQRALPFS VGARDGVLAT QGRLDREELC RGSDLCEVAF SVLYRKSGAM NCLRVRVEVM
DQNDHSPQFP NAEQDVEISE IAGLRMRIPL ERAVDPDAGP NGLQTYSLSV NRYFALDVTV
GPEGTKQAEL VIIRELDREV QDSVDLSLVA WDKGDPPRSG STLIHVRIQD SNDNSPTFED
SAPTVELPEN TARGTTIISL KATDPDQGVN GEVVYSLSKH TQPEVQRLIA VDPQTAAVSL
KAPLDYEVQT SYEVVVEARD RGPNAIPAYC KLHIKLLDVN DNAPRILADW DRSSFPGPTV
LEGAPKDTFL SLVTVLDADS GQNGKVKAQI LEGSGPFSLK HMQGGNYKIV TNGTLDREQV
TWYNLTLLAQ DYGDPPLSSV KHMSVQVVDE NDNAPVFSTN IYKASFEETN RTGYQMLKVE
AHDVDLDLSG RVSYFIRNVT GADVDAYFSI HQTSGVIRAQ HRLDYEESRS HSFIVEAIDQ
GHPPLSSSAT VQIQVQDVND NYPVIKEPKP RKGVASLSVP VNADKGEIVT ELGTHLDGTA
ASFPVDPRTR SGFLASTIKA EDADSGPNGA LSYRIAKGNH NRLFWLHEAT GQLFVNATNA
TQLIGQNFKL DIAVSDMGSP RLTTTMTLEV TFINLRDHLK NSSPGARGQL SFTMMVAICL
GATCLLLLLT IALVTTLCRP EKRDNRAYNC RQAESTYTRH PRRPQKNIRK SDIQLIPVVR
GRKDEPPPDD SESQLLPTSS LMSEDQKMGR EYTPAPSALN SSFHSQGRPE VDASPPQHSR
SLLKPGTIEL DGTLPHKSRN SSSSSTRSRT PKVQTHPDDP AEGPACSSSQ ATLRRPKNSE
SGGSDAEHQR MLRSLVRLSM AAFGDPIQLS SASPEVQVSR NELLLHQMLL VRGQLQPRTN
FRGNKYSTAG QSSSCSSCSC CSSCSSCSCC SCSSSSSLLS LLFLLVFVSC SSSSPSIFTA
SSYDLFADVG DPAWMARLSL PLATDYHDNV FIPNGASVPG GRVPSPGRKS PDKDGPLGGA
LLSEVSTLFE MLMTQKADAH PGPPPDVLYR LSAAYRRSLG LDGSGTTAGA KAARNSGNAE
QRPAVAPPTG RPQGGATAEA EHWKRLKGF
//
