ID A0A452C3N6_BALAS Unreviewed; 932 AA.
AC A0A452C3N6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Protocadherin gamma-A4 isoform X11 {ECO:0000313|RefSeq:XP_028017642.1};
GN Name=LOC103012669 {ECO:0000313|RefSeq:XP_028017642.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_028017642.1};
RN [1] {ECO:0000313|RefSeq:XP_028017642.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028017642.1};
RG RefSeq;
RL Submitted (JAN-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_028017642.1; XM_028161841.1.
DR AlphaFoldDB; A0A452C3N6; -.
DR OrthoDB; 5402790at2759; -.
DR Proteomes; UP000261681; Unplaced.
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:SF94; PROTOCADHERIN GAMMA-A4; 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; 6.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..932
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019184794"
FT TRANSMEM 689..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..133
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 134..242
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 243..347
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 348..452
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 453..562
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 579..682
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 803..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 100724 MW; 873D8A6668B7E755 CRC64;
MAASPYCPDC SRLIGICVLL GALWEIRAEH ILYSVPEELE NGSFVGNIAK DLGLEPQELA
ERGVRIVSRG RTQLFALNPR SGSLVTAGRI DREELCDRSP KCVVNLEILL EDKVKIFGVE
VEIIDVNDNA PNFGAEQREI KVAESENPGT RFPLPEAFDP DIGINSLQGY QLSSNGHFSL
DVQSGADGIK YPELVLERAL DREEEAVHHL VLTAFDGGDR VHSGTTRIHV TLVDTNDNAP
VFTQPEYHVS VRENVPVGSR LLTVKATDPD EGANGEVTYS FRKVRDKISQ LFQLNSLTGD
ITILGDLDYE DSGFYDIDVE AHDGPGLRAR SKILVTILDV NDNAPEVTVT SLTSSIQETS
SPGTVIALFN VHDSDSGENG LVTCSIPDNL PFTLEKTFGN YHRLLTHRTL DREEVSEYNI
TVTATDHGTP PLSTETHISL NVADVNDNPP AFPQASYLAY IPENNPRGAS IFSVTAHDPD
SNENSRVTYS LAEDTLQGAP LSSYVSINSD TGVLYALRSF DYEQVRDLQL LVTASDSGDP
PLSSNVSLSI FVLDQNDNTP EILYPALPTD GSTGVELAPR SAEPGYLVTK VVAVDRDSGQ
NAWLFYRLLK ASDPGLFAVG LHTGEVRTAR ALLDRDALKQ SLVVAVQDHG QPPLSATVTL
TVAVADSIPD VLTDLGSLKP SADPNDSGLT LYLVVAVAAV SCVFLAFIIV LLALRLRRWH
MSRLLQASGS RLASVPASHF VGVDGVRAFL QTYSHEVSLT ADSRRSHVIF PQPNYADTLI
SQESCEKSGP LLISQDLLER KGEPSLQQQA PPNTDWRFSQ AQRPGTSGSQ NGDETGTWPN
NQFDTEMLQA MILASASEAA DGSSTLGGGA GTMGLSARYG PQFTLQHVPD YRQNVYIPGS
NATLTNAAGK RDGKAPAGGN GNKKKSGKKE KK
//
