PCDH9_HUMAN
ID PCDH9_HUMAN Reviewed; 1237 AA.
AC Q9HC56; A2A6U1; Q5VT83; Q7Z3U0; Q8N3K7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Protocadherin-9;
DE Flags: Precursor;
GN Name=PCDH9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Kools P.F.J., van Roy F.;
RT "Identification and characterization of a novel human protocadherin gene
RT with high homology to a chromosome X-linked protocadherin.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 154-1237 (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP STRUCTURE BY NMR OF 243-352.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the CA domain of human protocadherin 9.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Potential calcium-dependent cell-adhesion protein.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HC56-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HC56-2; Sequence=VSP_035430;
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DR EMBL; AF169692; AAF89689.2; -; mRNA.
DR EMBL; AL834258; CAD38933.1; -; mRNA.
DR EMBL; BX537422; CAD97664.1; -; mRNA.
DR EMBL; AL603863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136626; AAI36627.1; -; mRNA.
DR EMBL; BC136627; AAI36628.1; -; mRNA.
DR CCDS; CCDS9443.1; -. [Q9HC56-2]
DR CCDS; CCDS9444.1; -. [Q9HC56-1]
DR RefSeq; NP_001305301.1; NM_001318372.1.
DR RefSeq; NP_001305302.1; NM_001318373.1.
DR RefSeq; NP_065136.1; NM_020403.4. [Q9HC56-2]
DR RefSeq; NP_982354.1; NM_203487.2. [Q9HC56-1]
DR RefSeq; XP_016876108.1; XM_017020619.1. [Q9HC56-1]
DR PDB; 2EE0; NMR; -; A=246-352.
DR PDBsum; 2EE0; -.
DR AlphaFoldDB; Q9HC56; -.
DR SMR; Q9HC56; -.
DR BioGRID; 111134; 43.
DR IntAct; Q9HC56; 12.
DR MINT; Q9HC56; -.
DR STRING; 9606.ENSP00000367096; -.
DR GlyConnect; 1969; 9 N-Linked glycans (4 sites).
DR GlyGen; Q9HC56; 15 sites, 9 N-linked glycans (4 sites).
DR iPTMnet; Q9HC56; -.
DR PhosphoSitePlus; Q9HC56; -.
DR BioMuta; PCDH9; -.
DR DMDM; 206729886; -.
DR EPD; Q9HC56; -.
DR MassIVE; Q9HC56; -.
DR MaxQB; Q9HC56; -.
DR PaxDb; Q9HC56; -.
DR PeptideAtlas; Q9HC56; -.
DR PRIDE; Q9HC56; -.
DR ProteomicsDB; 81639; -. [Q9HC56-1]
DR ProteomicsDB; 81640; -. [Q9HC56-2]
DR Antibodypedia; 2687; 91 antibodies from 21 providers.
DR DNASU; 5101; -.
DR Ensembl; ENST00000377865.7; ENSP00000367096.2; ENSG00000184226.15. [Q9HC56-1]
DR Ensembl; ENST00000544246.5; ENSP00000442186.2; ENSG00000184226.15. [Q9HC56-2]
DR GeneID; 5101; -.
DR KEGG; hsa:5101; -.
DR MANE-Select; ENST00000377865.7; ENSP00000367096.2; NM_203487.3; NP_982354.1.
DR UCSC; uc001vil.4; human. [Q9HC56-1]
DR CTD; 5101; -.
DR DisGeNET; 5101; -.
DR GeneCards; PCDH9; -.
DR HGNC; HGNC:8661; PCDH9.
DR HPA; ENSG00000184226; Tissue enriched (brain).
DR MIM; 603581; gene.
DR neXtProt; NX_Q9HC56; -.
DR OpenTargets; ENSG00000184226; -.
DR PharmGKB; PA33008; -.
DR VEuPathDB; HostDB:ENSG00000184226; -.
DR eggNOG; ENOG502QPMK; Eukaryota.
DR GeneTree; ENSGT00940000155079; -.
DR InParanoid; Q9HC56; -.
DR OMA; XGPLGPR; -.
DR PhylomeDB; Q9HC56; -.
DR TreeFam; TF320624; -.
DR PathwayCommons; Q9HC56; -.
DR SignaLink; Q9HC56; -.
DR BioGRID-ORCS; 5101; 9 hits in 1075 CRISPR screens.
DR ChiTaRS; PCDH9; human.
DR EvolutionaryTrace; Q9HC56; -.
DR GenomeRNAi; 5101; -.
DR Pharos; Q9HC56; Tbio.
DR PRO; PR:Q9HC56; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9HC56; protein.
DR Bgee; ENSG00000184226; Expressed in inferior vagus X ganglion and 185 other tissues.
DR ExpressionAtlas; Q9HC56; baseline and differential.
DR Genevisible; Q9HC56; HS.
DR GO; GO:0044291; C:cell-cell contact zone; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
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 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; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 6.
DR PROSITE; PS50268; CADHERIN_2; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1237
FT /note="Protocadherin-9"
FT /id="PRO_0000003994"
FT TOPO_DOM 24..814
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 815..835
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 836..1237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..142
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 143..252
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 253..358
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 365..469
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 470..572
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 573..675
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 679..784
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 849..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 775
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1013..1046
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.1"
FT /id="VSP_035430"
FT CONFLICT 907
FT /note="P -> A (in Ref. 2; CAD97664)"
FT /evidence="ECO:0000305"
FT CONFLICT 922
FT /note="P -> S (in Ref. 2; CAD97664)"
FT /evidence="ECO:0000305"
FT STRAND 255..262
FT /evidence="ECO:0007829|PDB:2EE0"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:2EE0"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:2EE0"
FT HELIX 297..302
FT /evidence="ECO:0007829|PDB:2EE0"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:2EE0"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:2EE0"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:2EE0"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:2EE0"
FT STRAND 324..338
FT /evidence="ECO:0007829|PDB:2EE0"
FT STRAND 340..349
FT /evidence="ECO:0007829|PDB:2EE0"
SQ SEQUENCE 1237 AA; 136064 MW; E2EA8FCC24735C7D CRC64;
MDLRDFYLLA ALIACLRLDS AIAQELIYTI REELPENVPI GNIPKDLNIS HINAATGTSA
SLVYRLVSKA GDAPLVKVSS STGEIFTTSN RIDREKLCAG ASYAEENECF FELEVVILPN
DFFRLIKIKI IVKDTNDNAP MFPSPVINIS IPENTLINSR FPIPSATDPD TGFNGVQHYE
LLNGQSVFGL DIVETPEGEK WPQLIVQQNL DREQKDTYVM KIKVEDGGTP QKSSTAILQV
TVSDVNDNRP 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 FAVDVDTGMN AELKYTIVSG
NNKGLFRIDP VTGNITLEEK PAPTDVGLHR LVVNISDLGY PKSLHTLVLV FLYVNDTAGN
ASYIYDLIRR TMETPLDRNI GDSSQPYQNE DYLTIMIAII AGAMVVIVVI FVTVLVRCRH
ASRFKAAQRS KQGAEWMSPN QENKQNKKKK RKKRKSPKSS LLNFVTIEES KPDDAVHEPI
NGTISLPAEL EEQSIGRFDW GPAPPTTFKP NSPDLAKHYK SASPQPAFHL KPDTPVSVKK
HHVIQELPLD NTFVGGCDTL SKRSSTSSDH FSASECSSQG GFKTKGPLHT RQCNSHSKSD
NIPVTPQKCP SSTGFHIQEN EESHYESQRR VTFHLPDGSQ ESCSDSGLGD HEPVGSGTLI
SHPLPLVQPQ DEFYDQASPD KRTEADGNSD PNSDGPLGPR GLAEATEMCT QECLVLGHSD
NCWMPPGLGP YQHPKSPLST FAPQKEWVKK DKLVNGHTLT RAWKEDSNRN QFNDRKQYGS
NEGHFNNGSH MTDIPLANLK SYKQAGGATE SPKEHQL
