PC11X_PIG
ID PC11X_PIG Reviewed; 1117 AA.
AC Q6KEQ9; Q6KEQ6; Q6KEQ8;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Protocadherin-11 X-linked;
DE Short=Protocadherin-11;
DE AltName: Full=Protocadherin on the X chromosome;
DE Short=PCDH-X;
DE Flags: Precursor;
GN Name=PCDH11X; Synonyms=PCDH11, PCDHX;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=15112107; DOI=10.1007/s00335-003-3034-9;
RA Blanco-Arias P., Sargent C.A., Affara N.A.;
RT "A comparative analysis of the pig, mouse, and human PCDHX genes.";
RL Mamm. Genome 15:296-306(2004).
CC -!- FUNCTION: Potential calcium-dependent cell-adhesion protein.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in adrenal gland, brain, heart, kidney,
CC lung, prostate, skeletal muscle, testis and thymus.
CC {ECO:0000269|PubMed:15112107}.
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DR EMBL; AJ564972; CAD92443.1; -; mRNA.
DR EMBL; AJ564973; CAD92444.1; -; mRNA.
DR EMBL; AJ564974; CAD92445.1; -; mRNA.
DR EMBL; AJ564975; CAD92446.1; -; mRNA.
DR AlphaFoldDB; Q6KEQ9; -.
DR SMR; Q6KEQ9; -.
DR STRING; 9823.ENSSSCP00000027762; -.
DR PaxDb; Q6KEQ9; -.
DR PRIDE; Q6KEQ9; -.
DR eggNOG; ENOG502QPMK; Eukaryota.
DR InParanoid; Q6KEQ9; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR013585; Protocadherin.
DR Pfam; PF00028; Cadherin; 6.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF08374; Protocadherin; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 7.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 7.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1117
FT /note="Protocadherin-11 X-linked"
FT /id="PRO_0000232763"
FT TOPO_DOM 24..812
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 834..1117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..139
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 140..249
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 250..355
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 362..466
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 467..570
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 571..673
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 677..795
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 1029..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1117 AA; 123364 MW; A90AE0AA297EB29C CRC64;
MDLLSGTHIF AVLLACIVFQ SGAQEKNYTI REEMPENVLI GDLLKDLNLS LIPDRSLTTP
MQFKLVYKTG DVPLIRIEEG TGEIFTTGAR IDREKLCAGI VVDAHCFYEV EVAVLPDEIF
RLVKIRFLIE DINDNAPLFP ATVINISIPE NSAINSRYAL PATIDPDTGI NGVQNYHLIK
GQSIFGLDVI ETPEGEKMPQ LIVQKELDRE EKDTYVMKIK VEDGGFPQRS STAILQVSVA
DTNDNRPVFK ENEIEVSIPE NAPVGSSVTQ LHATDADIGE NAKIHFYFSN LISNMAKKLF
HLNSTTGLIT IKEPLDREES PNHKLLVLAS DGGLTPARAM VLVNVTDIND NIPSIDIRYI
INPINGTVVL SENAPLNTKI ALITVTDKDA DHNGWVSCFT DHEVPFRLRP VFSNQFLLET
AAYLDYESTR EYAIKLLAAD AGKPPLNQSS MLLIKVKDEN DNAPVFTQPF LSLSVPENNS
PGTQLTKISA MDADSGRNAE INYLLGFDAP SEFNLDHRTG ILTAVKKLDR EKQEKYSFTV
LAKDNGMPPL MTNATVLVTV LDQNDNSPVF THNEYNFYVP ENLPRHGTVG LITVTDPDYG
ENSAVILSIL DANDDFTIDP QTGVIQPNIS FDREKQESYT FYVKAEDGGR ISRSSTAKVT
INVVDVNDNK PVFVVPSSNY SFELVPPSTN PGTVVFTVVA IDNDTGMNAE LRYSMVGGNT
KGLFIIDQTS GNITLKEKCV FADLGLHRLV VKAKDLGQPD SLFNVVNVNL FVNESVTNAT
LIYELVRKNI ETPVTQNIET TDASSPSSDY VKIVVAIVAG TITVILVIFI TAVVRCQQSP
HLKAAQKNKQ NSEWVTPNPE NRQMIMMKKK KKKKKKHAPK NLLLNFVTIE EAKADGADNN
RSSITLDLPI ELEEQTMGKY NWGTTPTTFK PDSADLARHY KSASPQPTFQ IQPETPLNSK
HHIIQELPLD NTFVGCDSIS KCSSSSSDPY SVSECSYPVT TFKTPVSVHT RPPMKEAIRF
HTPMKETTTV EIWTHPQPQR KSEGKRAGKS QRRVTFHLPE GSQESSSDGG LGDHDTGSLP
STSHALPLGY PQEEYFDHAA PNNRTEGDGN SDPESGK
