PCDBG_HUMAN
ID PCDBG_HUMAN Reviewed; 776 AA.
AC Q9NRJ7; B3KPK5; Q8IYD5; Q96SE9; Q9HCF1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 4.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Protocadherin beta-16 {ECO:0000305};
DE Short=PCDH-beta-16;
DE AltName: Full=Protocadherin-3X;
DE Flags: Precursor;
GN Name=PCDHB16 {ECO:0000312|HGNC:HGNC:14546};
GN Synonyms=KIAA1621 {ECO:0000303|PubMed:10997877}, PCDH3X;
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 [GENOMIC DNA / MRNA].
RX PubMed=11322959; DOI=10.1016/s0014-5793(01)02372-9;
RA Vanhalst K., Kools P., Vanden Eynde E., van Roy F.;
RT "The human and murine protocadherin-beta one-exon gene families show high
RT evolutionary conservation, despite the difference in gene number.";
RL FEBS Lett. 495:120-125(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-525 AND SER-532.
RX PubMed=11230163; DOI=10.1101/gr.167301;
RA Wu Q., Zhang T., Cheng J.-F., Kim Y., Grimwood J., Schmutz J., Dickson M.,
RA Noonan J.P., Zhang M.Q., Myers R.M., Maniatis T.;
RT "Comparative DNA sequence analysis of mouse and human protocadherin gene
RT clusters.";
RL Genome Res. 11:389-404(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-525 AND SER-532.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-525 AND SER-532.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ARG-525 AND
RP SER-532.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP PROTEIN SEQUENCE OF 518-525.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
CC -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May be
CC involved in the establishment and maintenance of specific neuronal
CC connections in the brain.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13447.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF217757; AAF81914.1; -; mRNA.
DR EMBL; AF282973; AAG10030.1; -; Genomic_DNA.
DR EMBL; AY013878; AAK21988.1; -; mRNA.
DR EMBL; AB046841; BAB13447.1; ALT_INIT; mRNA.
DR EMBL; AK056460; BAG51717.1; -; mRNA.
DR EMBL; AC074130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61975.1; -; Genomic_DNA.
DR EMBL; BC036062; AAH36062.1; -; mRNA.
DR CCDS; CCDS4251.1; -.
DR RefSeq; NP_066008.2; NM_020957.3.
DR AlphaFoldDB; Q9NRJ7; -.
DR SMR; Q9NRJ7; -.
DR BioGRID; 121740; 47.
DR IntAct; Q9NRJ7; 35.
DR STRING; 9606.ENSP00000477314; -.
DR GlyConnect; 1680; 1 N-Linked glycan (1 site).
DR GlyGen; Q9NRJ7; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9NRJ7; -.
DR PhosphoSitePlus; Q9NRJ7; -.
DR BioMuta; PCDHB16; -.
DR DMDM; 308153560; -.
DR jPOST; Q9NRJ7; -.
DR MassIVE; Q9NRJ7; -.
DR PaxDb; Q9NRJ7; -.
DR PeptideAtlas; Q9NRJ7; -.
DR PRIDE; Q9NRJ7; -.
DR ProteomicsDB; 82381; -.
DR Antibodypedia; 73991; 118 antibodies from 21 providers.
DR DNASU; 57717; -.
DR Ensembl; ENST00000609684.3; ENSP00000477314.1; ENSG00000272674.4.
DR GeneID; 57717; -.
DR KEGG; hsa:57717; -.
DR MANE-Select; ENST00000609684.3; ENSP00000477314.1; NM_020957.4; NP_066008.2.
DR UCSC; uc032vnl.2; human.
DR CTD; 57717; -.
DR DisGeNET; 57717; -.
DR GeneCards; PCDHB16; -.
DR HGNC; HGNC:14546; PCDHB16.
DR HPA; ENSG00000272674; Low tissue specificity.
DR MIM; 604967; gene.
DR MIM; 606345; gene.
DR neXtProt; NX_Q9NRJ7; -.
DR OpenTargets; ENSG00000272674; -.
DR PharmGKB; PA33032; -.
DR VEuPathDB; HostDB:ENSG00000272674; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000164093; -.
DR HOGENOM; CLU_006480_3_0_1; -.
DR InParanoid; Q9NRJ7; -.
DR OrthoDB; 300321at2759; -.
DR PhylomeDB; Q9NRJ7; -.
DR TreeFam; TF332299; -.
DR PathwayCommons; Q9NRJ7; -.
DR SignaLink; Q9NRJ7; -.
DR BioGRID-ORCS; 57717; 13 hits in 1028 CRISPR screens.
DR GeneWiki; PCDHB16; -.
DR GenomeRNAi; 57717; -.
DR Pharos; Q9NRJ7; Tdark.
DR PRO; PR:Q9NRJ7; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NRJ7; protein.
DR Bgee; ENSG00000272674; Expressed in corpus epididymis and 134 other tissues.
DR ExpressionAtlas; Q9NRJ7; baseline and differential.
DR Genevisible; Q9NRJ7; HS.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0007416; P:synapse assembly; TAS:UniProtKB.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR032455; Cadherin_C.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF16492; Cadherin_C_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Direct protein sequencing; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..776
FT /note="Protocadherin beta-16"
FT /id="PRO_0000003944"
FT TOPO_DOM 29..690
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..776
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..133
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 138..242
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 247..347
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 352..451
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 456..561
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 568..671
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 91
FT /note="D -> E (in dbSNP:rs17096969)"
FT /id="VAR_055587"
FT VARIANT 347
FT /note="V -> L (in dbSNP:rs28664170)"
FT /id="VAR_061068"
FT VARIANT 508
FT /note="A -> T (in dbSNP:rs17844648)"
FT /id="VAR_061069"
FT VARIANT 525
FT /note="Q -> R (in dbSNP:rs17844651)"
FT /evidence="ECO:0000269|PubMed:10997877,
FT ECO:0000269|PubMed:11230163, ECO:0000269|PubMed:14702039,
FT ECO:0000269|Ref.6"
FT /id="VAR_026478"
FT VARIANT 532
FT /note="G -> S (in dbSNP:rs2697532)"
FT /evidence="ECO:0000269|PubMed:10997877,
FT ECO:0000269|PubMed:11230163, ECO:0000269|PubMed:14702039,
FT ECO:0000269|Ref.6"
FT /id="VAR_026479"
FT CONFLICT 357
FT /note="P -> A (in Ref. 7; AAH36062)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="T -> I (in Ref. 3; BAB13447)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="A -> E (in Ref. 3; BAB13447, 4; BAG51717, 2;
FT AAK21988 and 6; EAW61975)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="R -> S (in Ref. 3; BAB13447, 4; BAG51717, 2;
FT AAK21988 and 6; EAW61975)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="F -> L (in Ref. 7; AAH36062)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="Q -> H (in Ref. 3; BAB13447)"
FT /evidence="ECO:0000305"
FT CONFLICT 652
FT /note="R -> C (in Ref. 3; BAB13447)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="A -> V (in Ref. 3; BAB13447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 776 AA; 84936 MW; 93EF1C641A1DE0FB CRC64;
MEIGWMHNRR QRQVLVFFVL LSLSGAGAEL GSYSVVEETE RGSFVANLGK DLGLGLTEMS
TRKARIISQG NKQHLQLKAQ TGDLLINEKL DREELCGPTE PCILHFQVLM ENPLEIFQAE
LRVIDINDHS PMFTEKEMIL KIPENSPLGT EFPLNHALDL DVGSNNVQNY KISPSSHFRV
LIHEFRDGRK YPELVLDKEL DREEEPQLRL TLTALDGGSP PRSGTAQVRI EVVDINDNAP
EFEQPIYKVQ IPENSPLGSL VATVSARDLD GGANGKISYT LFQPSEDISK TLEVNPMTGE
VRLRKQVDFE MVTSYEVRIK ATDGGGLSGK CTLLLQVVDV NDNPPQVTMS ALTSPIPENS
PEIVVAVFSV SDPDSGNNGK TISSIQEDLP FLLKPSVKNF YTLVTERALD REARAEYNIT
LTVTDMGTPR LKTEHNITVQ ISDVNDNAPT FTQTSYTLFV RENNSPALHI GSVSATDRDS
GTNAQVTYSL LPPQDPHLPL ASLVSINADN GHLFALRSLD YEALQAFEFR VGATDRGSPA
LSREALVRVL VLDANDNSPF VLYPLQNGSA PCTELVPRAA EPGYLVTKVV AVDGDSGQNA
WLSYQLLKAT EPGLFGVWAH NGEVRTARLL SERDAAKQRL VVLVKDNGEP PRSATATLHV
LLVDGFSQPF LPLPEAAPGQ TQANSLTVYL VVALASVSSL FLFSVLLFVA VRLCRRSRAA
SVGRCSMPEG PFPGRLVDVS GTGTLSQSYQ YEVCLTGGSE TSEFKFLKPI IPNFSP
