ID A0A3L8SUT4_CHLGU Unreviewed; 1099 AA.
AC A0A3L8SUT4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=Cadherin domain-containing protein {ECO:0000259|PROSITE:PS50268};
GN ORFNames=DV515_00002879 {ECO:0000313|EMBL:RLW09072.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW09072.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW09072.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW09072.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW09072.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLW09072.1}.
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DR EMBL; QUSF01000005; RLW09072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SUT4; -.
DR STRING; 44316.ENSEGOP00005006875; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 7.
DR Gene3D; 2.60.40.60; Cadherins; 7.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR013585; Protocadherin.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF253; PROTOCADHERIN-7; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF08374; Protocadherin; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 7.
DR SUPFAM; SSF49313; Cadherin-like; 7.
DR PROSITE; PS00232; CADHERIN_1; 4.
DR PROSITE; PS50268; CADHERIN_2; 7.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 878..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..146
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 147..296
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 297..403
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 418..524
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 525..634
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 635..742
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 745..849
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 186..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1099 AA; 118978 MW; 129EE5C23C8F59F3 CRC64;
MRKMRTLLRF VHCCCCCFLF LLPPPLWVSL AAAKQLLKYR LAEEGPADIR IGNVASDLGI
VTGSGEVTFS LESGSDYLKI DNMTGELSTT ERRIDREKLP QCQMIFDENE CFLDFEVSVI
GPSQSWVDLF EGRVIILDIN DNTPTFPSPV LTLTVEENRP VGTLYLLPTA TDRDFGRNGI
ERYELLQEPG GDGGRRGGGG GGAAAAAPES APFPGGSKRR QEAEAAARSS VFELQVADTL
DGEKQPQLIV KGALDREQRD SYELSLRVRD GGDPARSSQA ILRVLITDVN DNSPRFEKSV
YEADLAENSS PGTPILQLRA TDLDVGVNGQ IEYVFGAATE SVRRLLRLDE TSGWLSVLHR
IDREEVNQLR FTVMARDRGQ PPKTDKATVV LNIRDENDNV PTIDIRKIGR IPLRDGVASV
AEDVLVDTPI ALVQVSDRDQ GENGVVTCTV VGDVPFQLKP ASEGEGEPQN KRKYFLHTSA
PLDYEAVRDY NVVIVAVDSG SPSLSSNNSL LVRVGDTNDN PPMFSQAVLE VSFPENNLPG
ERVATVVATD ADSGKNAEIT YSLEASPLSS EAPGSIFSID PDSGDVSVQT VLDREQRDTY
EFQVTARDKG VPSLQGSTTV VVRVSDRNDN EPRFMQDVFT FYVKENLQPN SPVGMVTVMD
FDKGRNAELS LSIQPGDHEQ AAGIFSIEND TGTIFSTVSF DREQQTSYTF KVKAVDGGEP
PRSATATVSL FVMDENDNAP TVTFPSNSSY TVLPPSSNMR TVVATVVATD ADTGLNADLN
YSIVGGNPFK LFEIDPASGV VSLVGKLAPK HYGLHRLVVQ VNDSGQPPQS TTALLHVFVN
ESLSNATVVE SQVARSLHTP LAQDIAGDPS YELSKQRLSI VIGVVAGIMT VILLILVVVM
ARYCRSKGKH GYEAGKKDHE DFFTPQQHDK AKKPKKDKKG KKGKQPLYSS IVTVEASKPN
GQRYDSVNEK LSDSPGMGRY RSVNGGPGSP DLARHYKSSS PLPTVQLHPQ SPTAGKKHQA
VQDLPPANTF VGAGDNISIG SDHCSEYSCQ ASSKYSKQVR ALHPAGPSTP TLAHGAGEGA
GMPVPPPPTL AQAHTRQDQ
//
