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Database: UniProt
Entry: A0A1S3RT14_SALSA
LinkDB: A0A1S3RT14_SALSA
Original site: A0A1S3RT14_SALSA 
ID   A0A1S3RT14_SALSA        Unreviewed;       964 AA.
AC   A0A1S3RT14;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Protocadherin gamma-A3-like isoform X9 {ECO:0000313|RefSeq:XP_014055450.1};
GN   Name=LOC106604876 {ECO:0000313|RefSeq:XP_014055450.1};
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_014055450.1};
RN   [1] {ECO:0000313|RefSeq:XP_014055450.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014055450.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May be
CC       involved in the establishment and maintenance of specific neuronal
CC       connections in the brain. {ECO:0000256|ARBA:ARBA00003436}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   RefSeq; XP_014055450.1; XM_014199975.1.
DR   AlphaFoldDB; A0A1S3RT14; -.
DR   GeneID; 106604876; -.
DR   OrthoDB; 4163668at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa05.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IPR032455; Cadherin_C.
DR   InterPro; IPR031904; Cadherin_CBD.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   PANTHER; PTHR24028; CADHERIN-87A; 1.
DR   PANTHER; PTHR24028:SF296; PROTOCADHERIN DELTA 1; 1.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   Pfam; PF16492; Cadherin_C_2; 1.
DR   Pfam; PF15974; Cadherin_tail; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin-like; 6.
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};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        692..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..138
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          139..247
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          248..352
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          353..457
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          458..567
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          582..679
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          800..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          903..964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        903..937
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   964 AA;  106418 MW;  CB2C227B6552FFDB CRC64;
     MEFKGFRQPT TWRLCGLQWQ VHIFLLYLSH VVCGQIRYSI PEEMKKGSLI GNVAQDLGLD
     LKRLRAGRAR IVTGESIQYT ELKTDKGILV VSERIDREQL CGDVTPCSFS FEMILENPME
     LHRITVEILD VNDHAPAFPN KYIHFEISES ATVGSRFLLE SAEDNDVGLN ALQNYILTPN
     DNFILKQHTN PDGSKYAEMV LQKPLDREEN PRLSLKLIAV DGGNPQRSGS VNIEITVLDA
     NDNAPVFNQS VYRATVMENA LKSTYITTVN ASDADSGSNG YISYMFSNLK GTVSETFTID
     ANTGVISVLG EIDYEKYKKY EIRIDATDQG GLTDSSKVIV EVIDVNDNEP VISVMSFTSP
     ISEDSPHGTT IGIINVKDLD SGENGQVSCS IDQNIPFNIK SNVRNYYTLV TGAVLDRESV
     SEYNITVVAT DAGSPPLSSR RTFHLKVSDV NDNAPVFPQV VYNSYVAENN SPGVSIFTVT
     AKDTDSNQNA RISYILEDSD VSGTPVSVYV SVNAESGVIH AVRSFDYEQM KQLRLVVKAQ
     DGGSPPLSSN VTVIIFIQDQ NDNAPQVLYP VQTSSSLVAE MVPRSADVGY LVTKVVAVDV
     DSGQNAWLSY KLQKATDRAL FEVGLQNGEI RTIRQVTDKD AVKQRLTVVV EDNGQPSRSA
     TVNVNVAVAD SFPEVLSEFT DFTHDKEYND NLTFYLVLAL AVVSFLFITC LVVIISVKIY
     RWRQSRILYH SNLPVIPYYP PRYADTLGTG TLQHVYNYEV CRTTDSRKSD CQFARPCSQN
     VLIMDPSSTG TMQRIQNEKN ILDEPDSPLE QKPPNADWRF TQGQRPGPSG AGGPPEMAMG
     TGPWPNPPTE AEQLQALMAA ANEVSEATAT LGPGTMGLST RYSPQFTLQH VPDYRQNVYI
     PGSTATLTSN PQQQQQQQML MQQQMAAQHQ ALQAQPSEAA AQPEPPKPAQ TPASKKKSTK
     KEKK
//
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