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   13-FEB-2019, entry version 157.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA   Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA   Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA   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.,
RA   Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA   Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA   Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA   Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA   Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA   Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA   Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA   King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA   Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA   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.,
RA   Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA   Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA   Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA   Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA   Hubbard T., Sulston J.E., Beck S., Bentley D.R., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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
RT   patterning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:17849-17854(2007).
CC   -!- FUNCTION: Potential calcium-dependent cell-adhesion protein.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       type I 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         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay.;
CC   -!- DEVELOPMENTAL STAGE: During midgestation, enriched in the frontal
CC       and anterior temporal cortices. Expressed at high levels in the
CC       exterior margins of the thalamus, ventromedial striatal
CC       neuroepithelium and anterior cingulate.
CC       {ECO:0000269|PubMed:17978184}.
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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   UniGene; Hs.106511; -.
DR   ProteinModelPortal; O14917; -.
DR   SMR; O14917; -.
DR   BioGrid; 118101; 9.
DR   IntAct; O14917; 9.
DR   iPTMnet; O14917; -.
DR   PhosphoSitePlus; O14917; -.
DR   SwissPalm; O14917; -.
DR   BioMuta; PCDH17; -.
DR   EPD; O14917; -.
DR   jPOST; O14917; -.
DR   MaxQB; O14917; -.
DR   PaxDb; O14917; -.
DR   PeptideAtlas; O14917; -.
DR   PRIDE; O14917; -.
DR   ProteomicsDB; 48295; -.
DR   ProteomicsDB; 48296; -. [O14917-2]
DR   Ensembl; ENST00000377918; ENSP00000367151; ENSG00000118946. [O14917-1]
DR   Ensembl; ENST00000484979; ENSP00000432899; ENSG00000118946. [O14917-2]
DR   GeneID; 27253; -.
DR   KEGG; hsa:27253; -.
DR   UCSC; uc001vhq.2; human. [O14917-1]
DR   CTD; 27253; -.
DR   DisGeNET; 27253; -.
DR   EuPathDB; HostDB:ENSG00000118946.11; -.
DR   GeneCards; PCDH17; -.
DR   HGNC; HGNC:14267; PCDH17.
DR   HPA; HPA026817; -.
DR   MIM; 611760; gene.
DR   neXtProt; NX_O14917; -.
DR   OpenTargets; ENSG00000118946; -.
DR   PharmGKB; PA33001; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   eggNOG; ENOG410XQHI; LUCA.
DR   GeneTree; ENSGT00940000156894; -.
DR   HOGENOM; HOG000220893; -.
DR   HOVERGEN; HBG054878; -.
DR   InParanoid; O14917; -.
DR   KO; K16499; -.
DR   OMA; PQGHVGC; -.
DR   OrthoDB; 64478at2759; -.
DR   PhylomeDB; O14917; -.
DR   TreeFam; TF352008; -.
DR   ChiTaRS; PCDH17; human.
DR   GeneWiki; PCDH17; -.
DR   GenomeRNAi; 27253; -.
DR   PRO; PR:O14917; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   Bgee; ENSG00000118946; Expressed in 206 organ(s), highest expression level in upper lobe of lung.
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   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW   Complete proteome; Glycoprotein; Membrane; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   CHAIN        18   1159       Protocadherin-17.
FT                                /FTId=PRO_0000004001.
FT   TOPO_DOM     18    707       Extracellular. {ECO:0000255}.
FT   TRANSMEM    708    728       Helical. {ECO:0000255}.
FT   TOPO_DOM    729   1159       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       18    132       Cadherin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      133    243       Cadherin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      244    351       Cadherin 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      353    472       Cadherin 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      473    583       Cadherin 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      589    695       Cadherin 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   MOTIF       186    188       Cell attachment site. {ECO:0000255}.
FT   COMPBIAS    382    408       Gly-rich.
FT   CARBOHYD     22     22       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    266    266       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    439    439       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    453    453       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    504    504       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    566    566       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    590    590       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ     876    889       SSTFKDPERASLRD -> ISVAPRLRTQKEPA (in
FT                                isoform 2). {ECO:0000303|Ref.1}.
FT                                /FTId=VSP_021581.
FT   VAR_SEQ     890   1159       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.1}.
FT                                /FTId=VSP_021582.
FT   CONFLICT    139    139       M -> L (in Ref. 1; AAB84144).
FT                                {ECO:0000305}.
FT   CONFLICT    256    256       A -> T (in Ref. 1; AAB84144).
FT                                {ECO:0000305}.
FT   CONFLICT    330    330       P -> L (in Ref. 1; AAB84144).
FT                                {ECO:0000305}.
FT   CONFLICT    430    430       L -> M (in Ref. 1; AAB84144).
FT                                {ECO:0000305}.
FT   CONFLICT    489    489       E -> D (in Ref. 1; AAB84144).
FT                                {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
//