ID A0A3Q7SDN6_VULVU Unreviewed; 1263 AA.
AC A0A3Q7SDN6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=LOW QUALITY PROTEIN: protocadherin-7 {ECO:0000313|RefSeq:XP_025853271.1};
GN Name=PCDH7 {ECO:0000313|RefSeq:XP_025853271.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025853271.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025853271.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025853271.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025853271.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_025853271.1; XM_025997486.1.
DR STRING; 9627.ENSVVUP00000019124; -.
DR KEGG; vvp:112919126; -.
DR OrthoDB; 5353710at2759; -.
DR Proteomes; UP000286640; Unplaced.
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; 7.
DR Gene3D; 2.60.40.60; Cadherins; 8.
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 PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF253; PROTOCADHERIN-7; 1.
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; Cadherin-like; 7.
DR PROSITE; PS00232; CADHERIN_1; 4.
DR PROSITE; PS50268; CADHERIN_2; 7.
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:UP000286640};
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..1263
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018668388"
FT TRANSMEM 894..917
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..143
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 144..324
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 325..431
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 446..551
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 552..655
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 656..758
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 769..878
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 175..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 137482 MW; 88DD9E18A1D02C5B CRC64;
MLRMRTAGWA RGWCLGCCLL VPLSLSLAAA KQLLRYRLAE EGPADVRIGN VASDLGIVTG
SGEVTFSLES GSEYLKIDNL TGELSTSERR IDREKLPQCQ MIFDENECFL DFEVSVIGPS
QSWVDLFEGR VIVLDINDNT PTFPSPVLTL TVEENRPVGT LYLLPTATDR DFGRNGIERY
ELLQEPGGGG GGGEGRRAGX XXXXXXXXXX XXXXXXXGGP GGSRRRADAP EGGGPNPNAN
PNANANASPS AGAGGRSSVF ELQVADTPDG EKQPQLIVKG ALDREQRDSY ELTLRVRDGG
DPPRSSQAIL RVLITDVNDN SPRFEKSVYE ADLAENSAPG TPILQLRAAD LDVGVNGQIE
YVFGAATESV RRLLRLDETS GWLSVLHRID REEVNQLRFT VMARDRGQPP KTDKATVVLN
IKDENDNVPS IEIRKIGRIP LKDGVASVAE DVLVDTPIAL VQVSDRDQGE NGVVTCTVVG
DVPFQLKPAS DTEGDQNKKK YFLHTSAPLD YETTREFNVV IVAVDSGSPS LSSNNSLVVK
VGDTNDNPPV FGQSVVEVYF PENNVPGERV ATVLATDADS GKNAELAYSL DSAVVGTFAI
DPDSGDILVN TVLDREQTDR YEFKVNAKDK GIPVLQGSTT VIVQVADRND NDPKFMQDVF
TFYVKENLQP NSPVGMVTVM DADKGRNAEM SLYIEENSNI FSIENDTGTI YSTMSFDREH
QTTYTFRVKA VDGGDPPRSA TATVSLFVMD ENDNAPTVTL PRNISYTLLP PSSNVRTVVA
TVLATDSDDG INADLNYSIV GGNPFKLFEI DSTSGVVSLV GKLTQKHYGL HRLVVQVNDS
GQPSQSTTTL VHVFVNESVS NATVIDAQIA RSLHTPLTQD IAGDPSYEIS KQRLSIVIGV
VAGIMTVILI ILIVVMARYC RSKNKNGYEA GKKDHEDFFT PQQHDKSKKP KKDKKNKKSK
QPLYSSIVTV EASKPNGQRY DSVNEKLSDS PSMGRYRSVN GGPGSPDLAR HYKSSSPLPT
VQLHPQSPTA GKKHQAVQDL PPANTFVGAG DNISIGSDHC SEYSCQTNNK YSKQPFRRVT
FSVVSQPQDP HQGSLQSCYD SGLEESETPS SKSSSGPRLG ALPLPEDNYE RTTPDGSVDS
RPLPDVALTG KCTRECDEYG HSDSCWMPVR TSPERKKSQP KLSTFMPVDE RGSQEKLANG
EAAIMGDRNR NLLNKKLTSS YETFSAASFS KNEEANPEDI PLTKTGEYKP SPVNTLTRRE
VYL
//
