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CADHB_XENLA
ID   CADHB_XENLA             Reviewed;         884 AA.
AC   P33152;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 3.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Blastomere cadherin;
DE            Short=B-cadherin;
DE   AltName: Full=XBcad;
DE   Flags: Precursor;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7531482; DOI=10.1016/0925-4773(94)90040-x;
RA   Mueller H.-A.J., Kuehl M., Finnemann S., Schneider S., van der Poel S.Z.,
RA   Hausen P., Wedlich D.;
RT   "Xenopus cadherins: the maternal pool comprises distinguishable members of
RT   the family.";
RL   Mech. Dev. 47:213-223(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 438-884.
RX   PubMed=1840622; DOI=10.1016/0925-4773(91)90039-9;
RA   Herzberg F., Wildermuth V., Wedlich D.;
RT   "Expression of XBcad, a novel cadherin, during oogenesis and early
RT   development of Xenopus.";
RL   Mech. Dev. 35:33-42(1991).
CC   -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC       preferentially interact with themselves in a homophilic manner in
CC       connecting cells; cadherins may thus contribute to the sorting of
CC       heterogeneous cell types.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed in pituitary gland, lung and kidney.
CC   -!- DEVELOPMENTAL STAGE: During oogenesis and early development.
CC   -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC       cadherin domain and rigidify the connections, imparting a strong
CC       curvature to the full-length ectodomain. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA55292.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X78546; CAA55292.1; ALT_INIT; mRNA.
DR   EMBL; X63719; CAA45251.1; -; mRNA.
DR   PIR; S43064; S43064.
DR   RefSeq; NP_001089045.1; NM_001095576.1.
DR   AlphaFoldDB; P33152; -.
DR   SMR; P33152; -.
DR   BioGRID; 534745; 1.
DR   DNASU; 594865; -.
DR   GeneID; 594865; -.
DR   CTD; 594865; -.
DR   Xenbase; XB-GENE-864850; cdh3.L.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 594865; Expressed in gastrula and 16 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   Gene3D; 4.10.900.10; -; 1.
DR   InterPro; IPR039808; Cadherin.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR   InterPro; IPR014868; Cadherin_pro_dom.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   PANTHER; PTHR24027; PTHR24027; 1.
DR   Pfam; PF00028; Cadherin; 4.
DR   Pfam; PF01049; Cadherin_C; 1.
DR   Pfam; PF08758; Cadherin_pro; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 4.
DR   SMART; SM01055; Cadherin_pro; 1.
DR   SUPFAM; SSF49313; SSF49313; 6.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 4.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW   Glycoprotein; Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..157
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003727"
FT   CHAIN           158..884
FT                   /note="Blastomere cadherin"
FT                   /id="PRO_0000003728"
FT   TOPO_DOM        158..706
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        707..730
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        731..884
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          158..265
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          266..378
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          379..489
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          490..595
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          596..706
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   CARBOHYD        427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        560
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        683
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        438..440
FT                   /note="ILT -> NSA (in Ref. 2; CAA45251)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        677
FT                   /note="R -> Q (in Ref. 2; CAA45251)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        787
FT                   /note="V -> A (in Ref. 2; CAA45251)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        820
FT                   /note="D -> N (in Ref. 2; CAA45251)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        857
FT                   /note="D -> N (in Ref. 2; CAA45251)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        863
FT                   /note="D -> N (in Ref. 2; CAA45251)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        882
FT                   /note="Missing (in Ref. 2; CAA45251)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   884 AA;  97980 MW;  9B865D7EE1DCB75B CRC64;
     MGGTDKFRYP SVWLCGLLCL LQVVPSINVD VSGCQPGFSS ANYTFSVNRR ELERGRKLGK
     VNLVDCTTRK HGLYDVGDSR FRVLPDGTVL VKRHVKLHSK DTRFTISTWD ARGIKHSTNI
     SVVNKRHRSG EEARSRSSEL PVLTFPEKHT GLKRKKRDWV IPPIKVSENE RGPFPKRLVQ
     IKSNKEKLSK VFYSITGQGA DTPPEGIFRI EKETGWMQVT RPLDREEYEK YVLLSHAVSE
     NGASVEEPME ITVTVIDQND NRPKFTQPVF RGSVREGVQP GTKVMSVSAT DDDDSIDSLN
     GVIAYSILKQ DPEEPIPNLF TINRETGVIS LIGTGLDREK FPEYTLTVQA ADLDGAGLTA
     EGKAVIEITD ANDNAPIFDP KTYTALVPEN EVGFEVQRLS VTDLDMPGTA AWQAVYKIRV
     NEGGFFNITT DPESNQGILT TAKGLDFEVR KQYVIQITVE NAVPFSVPLP TSTATVTVTV
     EDVNEAPVFV PVVSRVDVSE DLTRGEKIVS LVAQDPDKQQ IQKLSYFIGN DPARWLTINK
     DNGIVTGNGN LDRESEYVKN NTYTVIMLVT DDGVPVGTGT GTLILHVLDI NDNGPVPSPR
     VFTMCDQNPE PQVLTITDAD IPPNTYPYSV SLSHGSELTW KAELDSKGTS MRLSPTQQLK
     KGDYSIYVLL ADAQANRQLT VVNATVCICE GKAIKCQEKL VAGFDLPIIL VILGSILALL
     ILSLLLLLFL KRKKVVKEPL LLPEDDTRDN IFYYGEEGGG EEDQDYDLSQ LHRGLDARPD
     IMRNDVVPTL MSVPHYRPRP SNPDEIGNFI DENLDAADND PTAPPYDSLL VFDYEGSGSE
     AASLSSLNSS NSNNEHDYNY LNDWGPRFRK LADMYGGDDD DDEE
 
 
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