ID   VSI10_XENLA             Reviewed;         527 AA.
AC   Q6GMZ9; Q52KX7;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=V-set and immunoglobulin domain-containing protein 10;
DE   Flags: Precursor;
GN   Name=vsig10;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH73724.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH94149.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BC073724; AAH73724.1; ALT_INIT; mRNA.
DR   EMBL; BC094149; AAH94149.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001085300.1; NM_001091831.1.
DR   AlphaFoldDB; Q6GMZ9; -.
DR   SMR; Q6GMZ9; -.
DR   PRIDE; Q6GMZ9; -.
DR   DNASU; 443689; -.
DR   GeneID; 443689; -.
DR   CTD; 443689; -.
DR   Xenbase; XB-GENE-5959361; vsig10.L.
DR   OrthoDB; 1221933at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 443689; Expressed in blastula and 17 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 4.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07679; I-set; 1.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF48726; SSF48726; 4.
DR   PROSITE; PS50835; IG_LIKE; 4.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..13
FT                   /evidence="ECO:0000255"
FT   CHAIN           14..527
FT                   /note="V-set and immunoglobulin domain-containing protein
FT                   10"
FT                   /id="PRO_0000395116"
FT   TOPO_DOM        23..409
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        431..527
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          14..111
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          123..212
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          216..306
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          310..399
FT                   /note="Ig-like C2-type 4"
FT   REGION          501..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        144..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        238..288
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        330..387
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   527 AA;  58303 MW;  09A2531173BF1EAF CRC64;
     MWTRRWIQFL VLCLHLWVTV EGYLGVFRGD VNETITLSCN NVTELTAWFK DNNSGVVLAC
     DGENSSDGRF SRINGSSLVI TMLQIQDEGN YSCSKCSEDK SSQAYIQLKV SSGPYNVLAD
     ISPTRTLPNG TIYTSVGSNL SFGCSSNSYP APDLEIVLQR TDANPEPFPS IKGNNFLQFN
     LINVASNYQG NYTCSAVNPL SGRKLNSTRQ LLVYRPPITS IKCYANNSLG FSKMLLSCSW
     PGGYPDPLLQ WEQDGKIIAN ESFAANTKDT LVTYLNSSSL RVRQQFQCSG KHLSTKENNM
     KTCQIQIDLP LLESQPMRTC FTGENVTLSC SVSGAVPSAT ITWLRNISDP ESDIQPGKKY
     LISQKDSLSY LTILNCSHEE DEGYYTCKAE NVLGIKEINV WLTVNKPHNI VGLVTALLLL
     FLLVVAIITG TVLYCDPQIY LKANPFRSGA TDVLVLVDSE DEENEEVFDT AESVQYTDIV
     PNVPPPAANG HLSKHEVMFH RPPESTSSDL FSEVSDDTGE ENQNEEI