ID   A0A1S3SU58_SALSA        Unreviewed;       818 AA.
AC   A0A1S3SU58;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Protocadherin beta-16-like {ECO:0000313|RefSeq:XP_014067868.1};
GN   Name=LOC106611808 {ECO:0000313|RefSeq:XP_014067868.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014067868.1};
RN   [1] {ECO:0000313|RefSeq:XP_014067868.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014067868.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_014067868.1; XM_014212393.1.
DR   AlphaFoldDB; A0A1S3SU58; -.
DR   GeneID; 106611808; -.
DR   KEGG; sasa:106611808; -.
DR   OrthoDB; 5402790at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa09.
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; 5.
DR   Gene3D; 2.60.40.60; Cadherins; 6.
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   PANTHER; PTHR24028; CADHERIN-87A; 1.
DR   PANTHER; PTHR24028:SF342; PROTOCADHERIN GAMMA-B1; 1.
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; Cadherin-like; 5.
DR   PROSITE; PS00232; CADHERIN_1; 3.
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:UP000087266};
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..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..818
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010222910"
FT   TRANSMEM        688..713
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..134
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          135..243
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          244..348
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          349..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          578..675
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
SQ   SEQUENCE   818 AA;  90266 MW;  313D1D3495A3C458 CRC64;
     MGDWRSTGRR GGWQVVFFFL CLCALDSVTG QARYSIPEEQ SEGSIVGNIG RDLGLEVKRL
     VSGKARIITK GARQYVDLNR DKGLLVVKER IDREELCGQT TPCSFSFELI IENPIQLYRV
     TVEVRDINDN APSFPKDEIN LEISENAVSG ARFSLESADD PDVGVNGIQN YSLKPADNFK
     LEVHSQADGG KYIEMILQTP LDREEQETLS LMLIATDGGE PQRTGTVRIH ITVLDANDNA
     PVCGQPVYKT DVKESSPKGT LITTVSANDA DQGVNGEVTF SIAHVAKEAK ELFELNVDTG
     EIKVVGKLDF EKTKNYQLNV KARDHGGFTD TCKVVIQITD ENDNVPTIQL MSFSNSIPED
     SPPGTTVAVI NVEDADSDGN GVVLCSINAD IPFKIESSLT DYYTIVTEST LDRETVSEYN
     VTITVSDEGT PPLSSNKNIT VKVSDVNDNP PKFDQPVYSN SIQENNSPGF SIFSVRAGDA
     DWGQNARVSY FLDDKQVNGV TASSFVSVNS ENGAIHAVRS FDYEQIKSFQ FNVTARDGGS
     PPLSSMVAVR ILVQDQNDNS PQVLYPVQTS SSLVAEMVPR SADVGYLVTK VVAVDVDSGQ
     NAWLSYKLQK ATDRALFEVG LQNGEIRTIR QVTDKDAVKQ RLTVVVEDNG QPSRSATVNV
     NVAVADSFPE VLSEFTDFTH DKDYNDNLTF YLVLALAVVS FLFITCLVVI ISVKIYRWRQ
     SRVLYHSNLP VIPYYPPRYA DTLGTGTLQH VYNYEVCRTT DSRKSDCKFV RPCSQNVLIM
     DPSSTGTMQR MQSENNILDE PDSPLEVSLM SLNYSKLH
//