CADH4_XENLA
ID CADH4_XENLA Reviewed; 922 AA.
AC P79883;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Cadherin-4;
DE AltName: Full=Maternally-expressed neural cadherin;
DE AltName: Full=XmN-cadherin;
DE Flags: Precursor;
GN Name=cdh4;
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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP FUNCTION.
RC TISSUE=Tail bud;
RX PubMed=8652409; DOI=10.1016/0925-4773(95)00469-6;
RA Tashiro K., Tooi O., Nakamura H., Koga C., Ito Y., Hikasa H., Shiokawa K.;
RT "Cloning and expression studies of cDNA for a novel Xenopus cadherin (XmN-
RT cadherin), expressed maternally and later neural-specifically in
RT embryogenesis.";
RL Mech. Dev. 54:161-171(1996).
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. Probably contributes in early embryos to
CC cell-type non-specific cell adhesion, but in post-neurula embryos may
CC be responsible for the development and/or maintenance of anterior
CC neural tissues, and may be used in adult frog for the development
CC and/or maintenance of neural, endodermal and reproductive organs.
CC {ECO:0000269|PubMed:8652409}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Expressed strongly in ovary, testis, brain, eye and
CC kidney, and weakly in stomach and intestine.
CC {ECO:0000269|PubMed:8652409}.
CC -!- DEVELOPMENTAL STAGE: In the egg, the mRNA occurred as a maternal mRNA
CC at a relatively high level, and its level became very low by the
CC neurula stage, then increased steadily thereafter.
CC {ECO:0000269|PubMed:8652409}.
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}.
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DR EMBL; S82457; AAB37685.2; -; mRNA.
DR RefSeq; XP_018093711.1; XM_018238222.1.
DR AlphaFoldDB; P79883; -.
DR SMR; P79883; -.
DR GeneID; 108702627; -.
DR KEGG; xla:108702627; -.
DR OrthoDB; 191117at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
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; 5.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..922
FT /note="Cadherin-4"
FT /id="PRO_0000042784"
FT TOPO_DOM 25..740
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 741..761
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 762..922
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 176..283
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 284..398
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 399..513
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 514..621
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 620..728
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 138..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
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 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 922 AA; 101173 MW; FEA7A95CBAF1B640 CRC64;
MTGGPGSSPL FLLLLTGALS GARSRALGAY DGNASVSSAC TPGFSADGYT ALVSPNIMEG
QKLLKVKFNG CSSGAQGIWY ETNNPDFKVG ADGAVYTARE VQIPAKQAKF IVAAWDHETP
EKWEAAIQLF VEETPLNQSQ YQTGSQSQES EQEQSQSGTL LPWRQHHKGL RRQKRDWVIP
PVNVPENSRG PFPQQLVLIR SDKDRDDTIR YSITGVGADQ PPMAIFNIDP IFGRMNVTRP
LDREERSSYH LRAHAVDING NKVENPIDLS IYVIDMNDNR PEFSSPIFNG SVDEASKPGT
YVMTVTAHDA DDINTSNGIV MYRIMDQSPQ SPSHDMFVIH SKTGVINTVA AGLDREKVQQ
YTVVIQATDM EGNLNHGLSN TATAIITVAD VNDNPPEFTR KMFIGEVPEN HVDVVVANLT
VVDRDQPYTS NWNAVFKIIS GDPDGHFTIK TDPVTNEGIV TVSKPVDYEM SKVFPLIVMV
TNQAPLASGI QMSLQSTAAV TVSVNDVNEA PYFPNRNEPI RKLEGESAGR LLITFSAVDP
DHSMQQVLRY SKISDPANWL AINTTNGQVS TTAVLDRESP FVKDDLYQAK FLATDNGNPP
ASGTGTLLIQ LIDINDNAPE LLPKDAQICE RPNGNGINIT AIDVDRKPSA DPFVFELPSV
PYTIRRNWTI HRINSIYARL SLQIGYLESG MYDVPVIVTD SGNPPLYNTS IIKVKVCPCD
NNGDCTTIGA VAAAGLGTGA IISILICIII LLSMVLLFVM WMKRREKERH TKQLLIDPED
DVRDNILKYD EEGGGEEDQD YDLSQLQQPE TLDHVLNKVA GVRRVDERPV GAEHQYPIRP
VIPHPGDIGD FITEGLRAAD NDPTAPPYDS LLVFDYEGSG STAGSVSSLN SSSSEDQDFD
YLNDWGPRFK KLADMYGGAD ED
