ID   PCDB6_HUMAN             Reviewed;         794 AA.
AC   Q9Y5E3; B2R8R9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2023, sequence version 2.
DT   24-JUL-2024, entry version 175.
DE   RecName: Full=Protocadherin beta-6 {ECO:0000305};
DE            Short=PCDH-beta-6 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=PCDHB6 {ECO:0000312|HGNC:HGNC:8691};
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], AND VARIANT VAL-446.
RX   PubMed=10380929; DOI=10.1016/s0092-8674(00)80789-8;
RA   Wu Q., Maniatis T.;
RT   "A striking organization of a large family of human neural cadherin-like
RT   cell adhesion genes.";
RL   Cell 97:779-790(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-446.
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLN-636 AND ASP-776.
RC   TISSUE=Thalamus;
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).
CC   -!- FUNCTION: Calcium-dependent cell-adhesion protein involved in cells
CC       self-recognition and non-self discrimination. Thereby, it is involved
CC       in the establishment and maintenance of specific neuronal connections
CC       in the brain. {ECO:0000250|UniProtKB:Q91XZ4}.
CC   -!- SUBUNIT: Forms homodimers in trans (molecules expressed by two
CC       different cells). Forms promiscuous heterodimers in cis (at the plasma
CC       membrane of the same cell) with other protocadherins.
CC       {ECO:0000250|UniProtKB:Q91XZ4}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q91XZ4};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q91XZ4}.
CC   -!- DOMAIN: Cadherin 1 to cadherin 4 domains mediate homophilic trans-
CC       interaction, the interaction with an identical protocadherin expressed
CC       by a neighboring cell. This is a head-to-tail interaction, the cadherin
CC       1 domain interacting with the cadherin 4 domain and the cadherin 2
CC       domain interacting the cadherin 3 domain of the other protocadherin.
CC       The cadherin 6 domain mediates promiscuous interactions with
CC       protocadherins on the same cell membrane. Each cadherin domain binds
CC       three calcium ions. {ECO:0000250|UniProtKB:Q91XZ4}.
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DR   EMBL; AF152499; AAD43760.1; -; mRNA.
DR   EMBL; AF217752; AAK51619.1; -; mRNA.
DR   EMBL; AK313482; BAG36266.1; -; mRNA.
DR   CCDS; CCDS4248.1; -.
DR   RefSeq; NP_001290074.1; NM_001303145.1.
DR   RefSeq; NP_061762.2; NM_018939.3.
DR   AlphaFoldDB; Q9Y5E3; -.
DR   SMR; Q9Y5E3; -.
DR   BioGRID; 121070; 35.
DR   IntAct; Q9Y5E3; 1.
DR   STRING; 9606.ENSP00000231136; -.
DR   GlyCosmos; Q9Y5E3; 4 sites, No reported glycans.
DR   GlyGen; Q9Y5E3; 4 sites.
DR   iPTMnet; Q9Y5E3; -.
DR   PhosphoSitePlus; Q9Y5E3; -.
DR   BioMuta; PCDHB6; -.
DR   DMDM; 13431374; -.
DR   jPOST; Q9Y5E3; -.
DR   MassIVE; Q9Y5E3; -.
DR   PaxDb; 9606-ENSP00000231136; -.
DR   PeptideAtlas; Q9Y5E3; -.
DR   ProteomicsDB; 86342; -.
DR   Antibodypedia; 27197; 47 antibodies from 10 providers.
DR   DNASU; 56130; -.
DR   Ensembl; ENST00000231136.4; ENSP00000231136.1; ENSG00000113211.6.
DR   Ensembl; ENST00000708361.1; ENSP00000517189.1; ENSG00000291679.1.
DR   GeneID; 56130; -.
DR   KEGG; hsa:56130; -.
DR   MANE-Select; ENST00000231136.4; ENSP00000231136.1; NM_018939.4; NP_061762.2.
DR   UCSC; uc003lir.4; human.
DR   AGR; HGNC:8691; -.
DR   CTD; 56130; -.
DR   GeneCards; PCDHB6; -.
DR   HGNC; HGNC:8691; PCDHB6.
DR   HPA; ENSG00000113211; Low tissue specificity.
DR   MIM; 604967; gene.
DR   MIM; 606332; gene.
DR   neXtProt; NX_Q9Y5E3; -.
DR   OpenTargets; ENSG00000113211; -.
DR   PharmGKB; PA33040; -.
DR   VEuPathDB; HostDB:ENSG00000113211; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000163433; -.
DR   InParanoid; Q9Y5E3; -.
DR   OMA; GREMEEN; -.
DR   OrthoDB; 5402790at2759; -.
DR   PhylomeDB; Q9Y5E3; -.
DR   TreeFam; TF332299; -.
DR   PathwayCommons; Q9Y5E3; -.
DR   SignaLink; Q9Y5E3; -.
DR   BioGRID-ORCS; 56130; 11 hits in 1106 CRISPR screens.
DR   GenomeRNAi; 56130; -.
DR   Pharos; Q9Y5E3; Tdark.
DR   PRO; PR:Q9Y5E3; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9Y5E3; Protein.
DR   Bgee; ENSG00000113211; Expressed in cortical plate and 110 other cell types or tissues.
DR   ExpressionAtlas; Q9Y5E3; baseline and differential.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
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:0009988; P:cell-cell recognition; ISS:UniProtKB.
DR   GO; GO:0007268; P:chemical synaptic transmission; TAS:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
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   InterPro; IPR050174; Protocadherin/Cadherin-CA.
DR   PANTHER; PTHR24028; CADHERIN-87A; 1.
DR   PANTHER; PTHR24028:SF104; PROTOCADHERIN BETA-6; 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; 6.
DR   SUPFAM; SSF49313; Cadherin-like; 5.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW   Membrane; Metal-binding; Proteomics identification; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250|UniProtKB:Q91XZ4"
FT   CHAIN           28..794
FT                   /note="Protocadherin beta-6"
FT                   /id="PRO_0000003924"
FT   TOPO_DOM        28..688
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XZ4"
FT   TRANSMEM        689..709
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        710..794
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XZ4"
FT   DOMAIN          34..132
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          137..241
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          246..345
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          350..449
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          454..559
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          566..669
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REGION          773..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        416
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        565
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        95..101
FT                   /evidence="ECO:0000250|UniProtKB:Q91XZ4"
FT   VARIANT         231
FT                   /note="V -> I (in dbSNP:rs3776096)"
FT                   /id="VAR_021879"
FT   VARIANT         232
FT                   /note="L -> F (in dbSNP:rs10076554)"
FT                   /id="VAR_033705"
FT   VARIANT         446
FT                   /note="A -> V (in dbSNP:rs246707)"
FT                   /evidence="ECO:0000269|PubMed:10380929,
FT                   ECO:0000269|PubMed:11322959"
FT                   /id="VAR_070665"
FT   VARIANT         636
FT                   /note="H -> Q (in dbSNP:rs246703)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_033706"
FT   VARIANT         747
FT                   /note="Y -> H (in dbSNP:rs17685621)"
FT                   /id="VAR_033707"
FT   VARIANT         776
FT                   /note="G -> D (in dbSNP:rs17844444)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_070666"
SQ   SEQUENCE   794 AA;  87322 MW;  2172E2D7B89C6775 CRC64;
     MMQTKVQNKK RQVAFFILLM LWGEVGSESI QYSVLEETES GTFVANLTKD LGLRVGELAS
     RGARVVFKGN RQHLQFDPQT HDLLLNEKLD REELCGSTEP CVLPFQVLLE NPLQFFQASL
     RVRDINDHAP EFPAREMLLK ISEITMPGKI FPLKMAHDLD TGSNGLQRYT ISSNPHFHVL
     TRNRSEGRKF PELVLDKPLD REEQPQLRLT LIALDGGSPP RSGTSEIQIQ VLDINDNVPE
     FAQELYEAQV PENNPLGSLV ITVSARDLDA GSFGKVSYAL FQVDDVNQPF EINAITGEIR
     LRKALDFEEI QSYDVDVEAT DGGGLSGKCS LVVRVLDVND NAPELTMSFF ISLIPENLPE
     ITVAVFSVSD ADSGHNQQVI CSIENNLPFL LRPSVENFYT LVTEGALDRE SRAEYNITIT
     VTDLGTPRLK TQQSITVQVS DVNDNAPAFT QTSYTLFVRE NNSPALHIGS VSATDRDSGI
     NAQVTYSLLP PQDPHLPLSS LVSINADNGH LFALRSLDYE ALQSFEFRVG ATDRGSPALS
     SEALVRLLVL DANDNSPFVL YPLQNGSAPC TELVPRAAEP GYLVTKVVAV DGDSGQNAWL
     SYQLLKATEL GLFGVWAHNG EVRTARLLSE RDAAKHRLVV LVKDNGEPPR SATATLHVLL
     VDGFSQPYLP LPEAAPAQAQ ADSLTVYLVV ALASVSSLFL FSVLLFVAVR LCRRSRAASV
     GRYSVPEGPF PGHLVDVSGT GTLSQSYQYK VCLTGGSETN EFKFLKPIMP NFPPQGTERE
     MEETPTSRNS FPFS
//