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   24-JAN-2024, entry version 180.
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   GlyCosmos; Q9NRJ7; 3 sites, 1 glycan.
DR   GlyGen; Q9NRJ7; 4 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NRJ7; -.
DR   PhosphoSitePlus; Q9NRJ7; -.
DR   SwissPalm; Q9NRJ7; -.
DR   BioMuta; PCDHB16; -.
DR   DMDM; 308153560; -.
DR   jPOST; Q9NRJ7; -.
DR   MassIVE; Q9NRJ7; -.
DR   PaxDb; 9606-ENSP00000477314; -.
DR   PeptideAtlas; Q9NRJ7; -.
DR   ProteomicsDB; 82381; -.
DR   Antibodypedia; 73991; 127 antibodies from 21 providers.
DR   DNASU; 57717; -.
DR   Ensembl; ENST00000609684.3; ENSP00000477314.1; ENSG00000272674.4.
DR   Ensembl; ENST00000708367.1; ENSP00000517193.1; ENSG00000291684.1.
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   AGR; HGNC:14546; -.
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   OMA; QVLMENP; -.
DR   OrthoDB; 5402790at2759; -.
DR   PhylomeDB; Q9NRJ7; -.
DR   TreeFam; TF332299; -.
DR   PathwayCommons; Q9NRJ7; -.
DR   SignaLink; Q9NRJ7; -.
DR   BioGRID-ORCS; 57717; 15 hits in 1106 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 135 other cell types or tissues.
DR   ExpressionAtlas; Q9NRJ7; baseline and differential.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
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   CDD; cd11304; Cadherin_repeat; 5.
DR   Gene3D; 2.60.40.60; Cadherins; 6.
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   PANTHER; PTHR24028; CADHERIN-87A; 1.
DR   PANTHER; PTHR24028:SF71; PROTOCADHERIN BETA-16; 1.
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; Cadherin-like; 6.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 6.
DR   Genevisible; Q9NRJ7; HS.
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
//