PCD17_HUMAN
ID PCD17_HUMAN Reviewed; 1159 AA.
AC O14917; A8K1R5; Q5VVW9; Q5VVX0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Protocadherin-17;
DE AltName: Full=Protocadherin-68;
DE Flags: Precursor;
GN Name=PCDH17; Synonyms=PCDH68, PCH68;
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 Jin P., Xu H., Israel D.;
RT "Human protocadherin 68.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=17978184; DOI=10.1073/pnas.0706128104;
RA Abrahams B.S., Tentler D., Perederiy J.V., Oldham M.C., Coppola G.,
RA Geschwind D.H.;
RT "Genome-wide analyses of human perisylvian cerebral cortical patterning.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:17849-17854(2007).
CC -!- FUNCTION: Potential calcium-dependent cell-adhesion protein.
CC -!- INTERACTION:
CC O14917; Q9Y3Q8: TSC22D4; NbExp=3; IntAct=EBI-947061, EBI-739485;
CC O14917; Q8IY57-5: YAF2; NbExp=3; IntAct=EBI-947061, EBI-12111538;
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=O14917-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14917-2; Sequence=VSP_021581, VSP_021582;
CC -!- DEVELOPMENTAL STAGE: During midgestation, enriched in the frontal and
CC anterior temporal cortices. Expressed at high levels in the exterior
CC margins of the thalamus, ventromedial striatal neuroepithelium and
CC anterior cingulate. {ECO:0000269|PubMed:17978184}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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DR EMBL; AF029343; AAB84144.1; -; mRNA.
DR EMBL; AK289980; BAF82669.1; -; mRNA.
DR EMBL; AL445216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471124; EAW52060.1; -; Genomic_DNA.
DR EMBL; BC028165; AAH28165.1; -; mRNA.
DR CCDS; CCDS31986.1; -. [O14917-1]
DR PIR; T09055; T09055.
DR RefSeq; NP_001035519.1; NM_001040429.2. [O14917-1]
DR RefSeq; XP_005266414.1; XM_005266357.2. [O14917-1]
DR PDB; 6VFT; X-ray; 3.71 A; A/B/C/D=18-464.
DR PDBsum; 6VFT; -.
DR AlphaFoldDB; O14917; -.
DR SMR; O14917; -.
DR BioGRID; 118101; 33.
DR IntAct; O14917; 14.
DR STRING; 9606.ENSP00000367151; -.
DR GlyGen; O14917; 7 sites.
DR iPTMnet; O14917; -.
DR PhosphoSitePlus; O14917; -.
DR SwissPalm; O14917; -.
DR BioMuta; PCDH17; -.
DR EPD; O14917; -.
DR jPOST; O14917; -.
DR MassIVE; O14917; -.
DR MaxQB; O14917; -.
DR PaxDb; O14917; -.
DR PeptideAtlas; O14917; -.
DR PRIDE; O14917; -.
DR ProteomicsDB; 48295; -. [O14917-1]
DR ProteomicsDB; 48296; -. [O14917-2]
DR Antibodypedia; 9916; 157 antibodies from 26 providers.
DR DNASU; 27253; -.
DR Ensembl; ENST00000377918.8; ENSP00000367151.3; ENSG00000118946.12. [O14917-1]
DR Ensembl; ENST00000484979.5; ENSP00000432899.1; ENSG00000118946.12. [O14917-2]
DR GeneID; 27253; -.
DR KEGG; hsa:27253; -.
DR MANE-Select; ENST00000377918.8; ENSP00000367151.3; NM_001040429.3; NP_001035519.1.
DR UCSC; uc001vhq.2; human. [O14917-1]
DR CTD; 27253; -.
DR DisGeNET; 27253; -.
DR GeneCards; PCDH17; -.
DR HGNC; HGNC:14267; PCDH17.
DR HPA; ENSG00000118946; Tissue enhanced (brain, lung, lymphoid tissue).
DR MIM; 611760; gene.
DR neXtProt; NX_O14917; -.
DR OpenTargets; ENSG00000118946; -.
DR PharmGKB; PA33001; -.
DR VEuPathDB; HostDB:ENSG00000118946; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000156894; -.
DR HOGENOM; CLU_006480_1_1_1; -.
DR InParanoid; O14917; -.
DR OMA; RDPSFMA; -.
DR OrthoDB; 64478at2759; -.
DR PhylomeDB; O14917; -.
DR TreeFam; TF352008; -.
DR PathwayCommons; O14917; -.
DR SignaLink; O14917; -.
DR BioGRID-ORCS; 27253; 8 hits in 1066 CRISPR screens.
DR ChiTaRS; PCDH17; human.
DR GeneWiki; PCDH17; -.
DR GenomeRNAi; 27253; -.
DR Pharos; O14917; Tbio.
DR PRO; PR:O14917; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; O14917; protein.
DR Bgee; ENSG00000118946; Expressed in endothelial cell and 177 other tissues.
DR ExpressionAtlas; O14917; baseline and differential.
DR Genevisible; O14917; HS.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030534; P:adult behavior; IEA:Ensembl.
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 GO; GO:0050805; P:negative regulation of synaptic transmission; IEA:Ensembl.
DR GO; GO:1904071; P:presynaptic active zone assembly; IEA:Ensembl.
DR GO; GO:2000807; P:regulation of synaptic vesicle clustering; IEA:Ensembl.
DR GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR030709; Protocadherin-17.
DR PANTHER; PTHR24028:SF41; PTHR24028:SF41; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1159
FT /note="Protocadherin-17"
FT /id="PRO_0000004001"
FT TOPO_DOM 18..707
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 708..728
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 729..1159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..132
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 133..243
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 244..351
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 353..472
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 473..583
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 589..695
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 858..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 186..188
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 858..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 876..889
FT /note="SSTFKDPERASLRD -> ISVAPRLRTQKEPA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_021581"
FT VAR_SEQ 890..1159
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_021582"
FT CONFLICT 139
FT /note="M -> L (in Ref. 1; AAB84144)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="A -> T (in Ref. 1; AAB84144)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="P -> L (in Ref. 1; AAB84144)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="L -> M (in Ref. 1; AAB84144)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="E -> D (in Ref. 1; AAB84144)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1159 AA; 126229 MW; F687502B563B4013 CRC64;
MYLSICCCFL LWAPALTLKN LNYSVPEEQG AGTVIGNIGR DARLQPGLPP AERGGGGRSK
SGSYRVLENS APHLLDVDAD SGLLYTKQRI DRESLCRHNA KCQLSLEVFA NDKEICMIKV
EIQDINDNAP SFSSDQIEMD ISENAAPGTR FPLTSAHDPD AGENGLRTYL LTRDDHGLFG
LDVKSRGDGT KFPELVIQKA LDREQQNHHT LVLTALDGGE PPRSATVQIN VKVIDSNDNS
PVFEAPSYLV ELPENAPLGT VVIDLNATDA DEGPNGEVLY SFSSYVPDRV RELFSIDPKT
GLIRVKGNLD YEENGMLEID VQARDLGPNP IPAHCKVTVK LIDRNDNAPS IGFVSVRQGA
LSEAAPPGTV IALVRVTDRD SGKNGQLQCR VLGGGGTGGG GGLGGPGGSV PFKLEENYDN
FYTVVTDRPL DRETQDEYNV TIVARDGGSP PLNSTKSFAI KILDENDNPP RFTKGLYVLQ
VHENNIPGEY LGSVLAQDPD LGQNGTVSYS ILPSHIGDVS IYTYVSVNPT NGAIYALRSF
NFEQTKAFEF KVLAKDSGAP AHLESNATVR VTVLDVNDNA PVIVLPTLQN DTAELQVPRN
AGLGYLVSTV RALDSDFGES GRLTYEIVDG NDDHLFEIDP SSGEIRTLHP FWEDVTPVVE
LVVKVTDHGK PTLSAVAKLI IRSVSGSLPE GVPRVNGEQH HWDMSLPLIV TLSTISIILL
AAMITIAVKC KRENKEIRTY NCRIAEYSHP QLGGGKGKKK KINKNDIMLV QSEVEERNAM
NVMNVVSSPS LATSPMYFDY QTRLPLSSPR SEVMYLKPAS NNLTVPQGHA GCHTSFTGQG
TNASETPATR MSIIQTDNFP AEPNYMGSRQ QFVQSSSTFK DPERASLRDS GHGDSDQADS
DQDTNKGSCC DMSVREALKM KTTSTKSQPL EQEPEECVNC TDECRVLGHS DRCWMPQFPA
ANQAENADYR TNLFVPTVEA NVETETYETV NPTGKKTFCT FGKDKREHTI LIANVKPYLK
AKRALSPLLQ EVPSASSSPT KACIEPCTST KGSLDGCEAK PGALAEASSQ YLPTDSQYLS
PSKQPRDPPF MASDQMARVF ADVHSRASRD SSEMGAVLEQ LDHPNRDLGR ESVDAEEVVR
EIDKLLQDCR GNDPVAVRK
