ID A0A452EX32_CAPHI Unreviewed; 1016 AA.
AC A0A452EX32;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cadherin domain-containing protein {ECO:0000259|PROSITE:PS50268};
GN Name=PCDH9 {ECO:0000313|Ensembl:ENSCHIP00000016592.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000016592.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000016592.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000016592.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR EMBL; LWLT01000013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452EX32; -.
DR Ensembl; ENSCHIT00000024399.1; ENSCHIP00000016592.1; ENSCHIG00000016798.1.
DR GeneTree; ENSGT00940000155079; -.
DR Proteomes; UP000291000; Chromosome 12.
DR Bgee; ENSCHIG00000016798; Expressed in prefrontal cortex and 5 other cell types or tissues.
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; 7.
DR Gene3D; 2.60.40.60; Cadherins; 7.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR013585; Protocadherin.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF248; PROTOCADHERIN-9; 1.
DR Pfam; PF00028; Cadherin; 6.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF08374; Protocadherin; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 7.
DR SUPFAM; SSF49313; Cadherin-like; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 7.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1016
FT /note="Cadherin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018971246"
FT TRANSMEM 812..836
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..142
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 143..252
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 253..358
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 365..469
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 470..572
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 573..675
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 687..784
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 849..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 111694 MW; 8DDE9BAF5846DEFB CRC64;
MDLRDFYLLA ALIACLRLDS AIAQELIYTI REELPENIPI GNIPKDLNIS HINAATGTSA
SLVYRLVSKA GDAPLVKVSS STGEIFTTSN RIDREKLCAG ASYAEENECF FELEVVILPN
DFFRLIKIKI IVKDTNDNAP MFPSPVINIS IPENTLINSR FPIPSATDPD TGFNGVQHYE
LLNGQSVFGL DIVETPEGEK WPQLIVQQNL DREQKDTYVM KIKVEDGGTP QKSSTAILQV
TVSDVNDNKP VFKEGQVEVH IPENAPVGTS VIQLHATDAD IGSNAEIRYI FGAQVAPATK
RLFALNNTTG LITVQRSLDR EETAIHKVTV LASDGSSTPA RATVTINVTD VNDNPPNIDL
RYIISPINGT VYLSEKDPVN TKIALITVSD KDTDVNGKVI CFIEREVPFH LKAVYDNQYL
LETSSLLDYE GTKEFSFKIV ASDSGKPSLN QTALVRVKLE DENDNPPIFN QPVIELSVSE
NNRRGLYLTT ISATDEDSGK NADIVYQLGP NASFFDLDRK TGVLTASRVF DREEQERFIF
TVTARDNGTP PLQSQAAVIV TVLDENDNSP KFTHNHFQFF VSENLPKYST VGVITVTDAD
AGENKAVTLS ILNDNDNFVL DPYSGVIKSN VSFDREQQSS YTFDVKATDG GQPPRSSTAK
VTINVMDVND NSPVVISPPS NTSFKLVPLS AIPGSVVAEV FAVDIDTGMN AELKYTIVSG
NNKGLFRIDP VTGNITLEEK PAPTDVGLHR LVVNISDLGY PKSLHTLVLV FLYVNDTAGN
ASYIYDLIRR TMETPLDRNI GDSSQPYQNE DYLTIMIAIV AGAMVVIVVI FVTVLVRCRH
ASRFKAAQRS KQGAEWMSPN QENKQNKKKK RKKRKSPKSS LLNFVTIEES KPDDAVHEPI
NGTISLPAEL EEQSIGRFDW GPAPPTTFKP NSPDLAKHYK SASPQPAFHL KPDTPVSVKK
HHVIQELPLD NTFVGGCDTL SKRSSTSSDH FSASECSSQG GFKTKGPLHT RQAVEE
//
