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PCDBE_PANTR
ID   PCDBE_PANTR             Reviewed;         798 AA.
AC   Q5DRD5;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Protocadherin beta-14;
DE            Short=PCDH-beta-14;
DE   Flags: Precursor;
GN   Name=PCDHB14;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=15744052; DOI=10.1534/genetics.104.037606;
RA   Wu Q.;
RT   "Comparative genomics and diversifying selection of the clustered
RT   vertebrate protocadherin genes.";
RL   Genetics 169:2179-2188(2005).
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: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
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DR   RefSeq; NP_001019302.1; NM_001024131.2.
DR   AlphaFoldDB; Q5DRD5; -.
DR   SMR; Q5DRD5; -.
DR   STRING; 9598.ENSPTRP00000029638; -.
DR   PaxDb; Q5DRD5; -.
DR   PRIDE; Q5DRD5; -.
DR   GeneID; 471666; -.
DR   KEGG; ptr:471666; -.
DR   CTD; 56122; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   HOGENOM; CLU_006480_3_0_1; -.
DR   InParanoid; Q5DRD5; -.
DR   OrthoDB; 300321at2759; -.
DR   TreeFam; TF332299; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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:0007399; P:nervous system development; IEA:UniProt.
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; 6.
DR   SUPFAM; SSF49313; SSF49313; 6.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   3: Inferred from homology;
KW   Calcium; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..798
FT                   /note="Protocadherin beta-14"
FT                   /id="PRO_0000003941"
FT   TOPO_DOM        27..686
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        687..711
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        712..798
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        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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   DISULFID        96..102
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   798 AA;  87414 MW;  453EB0A4A0D605C3 CRC64;
     MEIRGALDLR KRQVLIFLVL LGLSRAGTES AHYSVAEETE IGSFVANLAR DLGLGVEELS
     SREARVVSDD NKKYLHLDLL TGNLLLNEKL DRDELCGSTE PCVLHFQVVL ENPLQFFRVE
     LRVKDINDHS PTFLDKEILI KISEGTTVGA TFLMESAQDL DVGSNSLQNY TISPNSHFYI
     KIPDSSDRKI YPELVLDRAL DYEQEAELRL TLTAVDGGSP PKSGTTLVLI KVLDINDNAP
     EFPQSLYEVQ VPEDRPLGSW IATISAKDLD AGNYGKISYT FFHASEDIRK TFEINPISGE
     VNLRSPLDFE VIQSYTINIQ ATDGGGLSGK CTLLVKVMDI NDNPPEVTIS SITKRIPENA
     SETLVALFSI LDQDSGDNGR MICSIQDNLP FFLKPTFKNF FTLVSEKALD RESQAEYNIT
     ITVTDLGTPR LKTEYNITVL VSDVNDNAPA FTQTSYTLFL RENNSPALHI GSVSATDRDS
     GTNAQVTYSL LPPQDPQLPL ASLVSINADN GHLFALRSLD YEALQEFEFR VGATDRGSPA
     LSSEALVRVL VLDANDNSPF VLYPLQNGSA PCTELVPRAA EPGYLVTKVV AVDGDSGQNA
     WLSYQLLKAT EPGLFGVWAH NGEVRTARLL SERDAAKHRL VVLVKDNGEP PRSATATLHV
     LLVDGFSQPY LPLPEAAPAQ AQADSLTVYL VVALASVSSL FLFSVLLFVA VRLCRRSRAA
     SVGRCSVPEG PFPGHLVDVS GTGTLSQSYQ YEVCLTGGSG TNEFKFLKPI IPNFQVHDTG
     KNMGEIENFR NSFGLNIQ
 
 
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