ID A0A2U3XJ78_LEPWE Unreviewed; 1004 AA.
AC A0A2U3XJ78;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Protocadherin alpha-C2 isoform X1 {ECO:0000313|RefSeq:XP_006731539.1};
GN Name=LOC102736751 {ECO:0000313|RefSeq:XP_006731539.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006731539.1};
RN [1] {ECO:0000313|RefSeq:XP_006731539.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006731539.1};
RG RefSeq;
RL Submitted (NOV-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}.
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_006731539.1; XM_006731476.2.
DR AlphaFoldDB; A0A2U3XJ78; -.
DR STRING; 9713.A0A2U3XJ78; -.
DR GeneID; 102736751; -.
DR KEGG; lww:102736751; -.
DR OrthoDB; 4259465at2759; -.
DR Proteomes; UP000245341; 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:SF119; PROTOCADHERIN ALPHA-C2; 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:UP000245341};
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..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..1004
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015669794"
FT TRANSMEM 703..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..145
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 146..254
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 255..362
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 371..466
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 467..576
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 591..688
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 881..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1004
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1004 AA; 108603 MW; 01B79CDD7C6DE831 CRC64;
MELAGPRPGA TEHPRLRPPM SWLLPPLPLL LLLLGPAASQ LRYSVPEEQA PGAPVGNVAS
ALGLELRRLG PGCLRINHLG APSPRYLELD LTSGALFVNE RIDREALCEQ RPRCLLSLEV
LAHSPVAVSA VEVEVLDIND NSPRFPRPDY QLQVSESVAP GARFHIESAQ DPDVGANSVQ
TYELSPSEHF ELDLKPLQEN SKVLELVLRK GLDREQAALH HLVLTAVDGG SPARSGTAQI
SVRVLDTNDN SPTFDQSTYR VQLREDAPPG TLVVKLNASD PDEGSNGELR YSLSSYTSDR
ERQLFSIDAS TGEVRVSGAL DYEEASSYQI YVQATDQGPV PMVGHCKVLV DIVDVNDNAP
EVVLTDLYSP VPEDAASNTV VALLSVNDQD SGLNRKVSLG LQASLPFRLN GFGSSYTLVV
SGPLDRERVA AYNITVTAAD GGVPQLTSQR TLQVEISDIN DNPPSFRQDS YSIYIEENNL
PGVLLCTVQA TDPDEKENAE VTYSLLEREV QGLPVTSYVS VNSASGSLYA VNSFDYEKFR
EFFVTVEAQD KGSPPLSSTV TANVYVVDMN DHAPHILYPT STNASAAIEM VPRTAPAGYL
VTKVIAMDSD SGQNAWLFYH LAQTSELDLF KVELHTGEIR TTRKMGDESG TTFNLTVVVR
DNGEPSLSSS VAITVAVVER VSRILPDTQR HVKSPRTYSE ITLYLIIALS TVSFIFLLTI
IVLSIIKCYR STAYGTACCG GFCGVRERCP AELNKQANNN IEARIPHGLK VQPHFIEVRG
NGSLTKTYCY KACLTAGSGS DTFMFYNTGA QTGLGPGGAQ AAASESRHLT GQSGQSAGNL
IILKNDAVSQ NEPRQPNPDW RYSASLRAGM HSSVHLEEAG ILRAGPGGPD QQWPTVSSAT
PEPEAGEVSP PVGAGVNSNS WTFKYGPGNP KQSGPGELPD KFIIPGSPAI ISIRQEPTNS
QIDKSDFITF GKKEETKKKK KKKKGNKTQE KKEKGNSTTD NSDQ
//
