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Database: UniProt
Entry: A0A1S3GPD0_DIPOR
LinkDB: A0A1S3GPD0_DIPOR
Original site: A0A1S3GPD0_DIPOR 
ID   A0A1S3GPD0_DIPOR        Unreviewed;      1100 AA.
AC   A0A1S3GPD0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Protocadherin-19 isoform X3 {ECO:0000313|RefSeq:XP_012890545.1};
GN   Name=Pcdh19 {ECO:0000313|RefSeq:XP_012890545.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012890545.1};
RN   [1] {ECO:0000313|RefSeq:XP_012890545.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012890545.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   RefSeq; XP_012890545.1; XM_013035091.1.
DR   AlphaFoldDB; A0A1S3GPD0; -.
DR   GeneID; 105999924; -.
DR   CTD; 57526; -.
DR   OrthoDB; 4259465at2759; -.
DR   Proteomes; UP000081671; Unplaced.
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; 6.
DR   Gene3D; 2.60.40.60; Cadherins; 6.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   PANTHER; PTHR24028; CADHERIN-87A; 1.
DR   PANTHER; PTHR24028:SF40; PROTOCADHERIN-19; 1.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; Cadherin-like; 5.
DR   PROSITE; PS00232; CADHERIN_1; 2.
DR   PROSITE; PS50268; CADHERIN_2; 6.
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:UP000081671};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1100
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010233649"
FT   TRANSMEM        679..701
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..129
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          130..238
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          239..346
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          350..453
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          454..563
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          569..672
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          851..873
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1051..1100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        854..873
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1064..1100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1100 AA;  121016 MW;  02BF7795A3F14EBE CRC64;
     MESLLLPVLL LLAVLWTQAA ALINLKYSVE EEQRAGTVIA NVAKDAREAG FALDPRQASA
     FRVVSNSAPH LVDINPSSGL LVTKQKIDRD LLCRQSPKCI ISLEVMSSSM EICVIKVEIK
     DLNDNAPSFP AAQIELEISE AASPGTRIPL DSAYDPDSGS FGVQTYELTP NELFGLEIKT
     RGDGSRFAEL VVEKSLDRET QSHYSFRITA LDGGDPPHLG TVGLSIKVTD SNDNNPVFGE
     STYAVSVPEN SPPNTPVIRL NASDPDEGTN GQVVYSFYGY VNDRTRELFQ IDPHSGLVTV
     TGALDYEEGH VYELDVQAKD LGPNSIPAHC KVTVSVLDTN DNPPVINLLS VNSELVEVSE
     SAPPGYVIAL VRVSDRDSGL NGRVQCRLLG NVPFRLQEYE SFSTILVDGR LDREQHDQYN
     LTIQARDGGV PMLQSAKSFT VRITDENDNH PHFSKPYYQV IVQENNTPGA YLLSVSARDP
     DLGLNGSVSY QIVPSQVRDM PVFTYVSINP NSGDIYALRS FNHEQTKAFE FKVLAKDGGL
     PSLQSNATVR VIILDVNDNT PVITAPPLIN GTAEVYIPRN SGIGYLVTVV KADDYDEGEN
     GRVTYDMTEG DRGYFEIDQV NGEVRTTRTF SESSKASYEL IVVAHDHGKT SLSASALVLI
     YLSPALDAQE SMGSVNLSLI FIIALGSIAG ILFVTMIFVA IKCKRDNKEI RTYNCRIAEY
     SYGHQKKSSK KKKISKNDIR LVPRDVEETD KMNVVSCSSL TSSLNYFDYH QQTLPLGCRR
     SESTFLNVEN QNTRNTSANH IYHHSFNSQG PQQPDLIING VPLPETENYS FDSNYVNSRA
     HLIKSSTFKD LEGNSLKDSG HEESDQTDSE HDVQRSLYCD TAVNDVLNTS VTSMGSQMPD
     HDQNEGFHCR EECRILGHSD RCWMPRNPMP TRSKSPEHVR NIIALSIEAT AADVEAYDDC
     GPTKRTFATF GKDVNDHPAE ERPTLKGKRT VDVTICSPKV NGAIREAGNG CEAISPVTSP
     LHLKSPLPTK PSMSYTLALA PQARDLEQYV NNVNNGPSRP SEAEPRGADS EKAMQEINPV
     LKEGRDKESP GVKRLKDIVL
//
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