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Database: UniProt
Entry: I3M604_ICTTR
LinkDB: I3M604_ICTTR
Original site: I3M604_ICTTR 
ID   I3M604_ICTTR            Unreviewed;       579 AA.
AC   I3M604;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Membrane frizzled-related protein {ECO:0000313|Ensembl:ENSSTOP00000004836.2};
GN   Name=MFRP {ECO:0000313|Ensembl:ENSSTOP00000004836.2};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000004836.2, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000004836.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR   EMBL; AGTP01052994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005328429.1; XM_005328372.1.
DR   AlphaFoldDB; I3M604; -.
DR   Ensembl; ENSSTOT00000005404.3; ENSSTOP00000004836.2; ENSSTOG00000005406.3.
DR   GeneID; 101971128; -.
DR   CTD; 83552; -.
DR   eggNOG; KOG3577; Eukaryota.
DR   eggNOG; KOG4292; Eukaryota.
DR   GeneTree; ENSGT00940000154525; -.
DR   HOGENOM; CLU_032137_0_0_1; -.
DR   OMA; WMCDLWR; -.
DR   OrthoDB; 5317198at2759; -.
DR   TreeFam; TF316506; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd07066; CRD_FZ; 1.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00112; LDLa; 2.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR24251:SF36; MEMBRANE FRIZZLED-RELATED PROTEIN; 1.
DR   PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF01392; Fz; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00063; FRI; 1.
DR   SMART; SM00192; LDLa; 2.
DR   SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 2.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        65..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          143..252
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          300..413
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          461..579
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   REGION          97..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        259..271
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        266..284
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        278..293
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        420..432
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        427..445
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        439..454
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   579 AA;  62177 MW;  6175AA4E88ADC7C5 CRC64;
     MKEYSDVILC MEATELSKTE FCNPAFEPEA GLPGPSAALR QDASHNIQAP WHGRRPRGLQ
     PDCHFSWLCI LLLASLLLLL LGLLAAIILS QLPAAPPPGA TKSPLPAQGL TTTTTPTTST
     STTSSATSGQ QGADASPAHQ ATCGGLLPGP RGFFSSPNYP DPYPPNAHCV WHIQVATDHT
     IQLKIEALSV EGVAACLFDR LEISPEPEGP LLRVCGKVPP PTLNTNASRL QVAFVSDSSV
     EGSGFQAWYQ AVAPGHGSCA HEEFHCDQLV CLLPDSVCDG FANCADGSDE TNCSAKLLGC
     GGNLTGLQGT FSTPSDLQQH PHQQLCTWHI SVPVGHGIEL QFWNFSLEAQ DECKFDYVEV
     YETSSSGALS LLGRFCGAET PPHLVSSHHE LAVLFRTDHS ISSGGFSATF KAFNATENPC
     GPRKFLCQNG GCRDLQWMCD LWRDCIDGNN DKNCSSPLLP PPELACEPVQ VEMCIGLSYN
     TTAFPNIWVG MATQEEVVDV LRGYKSLTSL PCYQNFRRLL CGLLVPRCTL LGSVLPPCRS
     VCQEAERQCQ SGLALLGTPW PFNCNRLPEA AGLEACAQP
//
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