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VSXL2_MOUSE
ID   VSXL2_MOUSE             Reviewed;         776 AA.
AC   A0A140LHF2;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 2.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=V-set and immunoglobulin domain-containing protein 10-like 2 {ECO:0000250|UniProtKB:P0DP72};
DE   Flags: Precursor;
GN   Name=Vsig10l2 {ECO:0000250|UniProtKB:P0DP72};
GN   Synonyms=Gm1113 {ECO:0000312|MGI:MGI:2685959};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
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DR   EMBL; AC118232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A140LHF2; -.
DR   GlyGen; A0A140LHF2; 2 sites.
DR   ProteomicsDB; 297827; -.
DR   Ensembl; ENSMUST00000183573; ENSMUSP00000146390; ENSMUSG00000098590.
DR   MGI; MGI:2685959; Gm1113.
DR   VEuPathDB; HostDB:ENSMUSG00000098590; -.
DR   GeneTree; ENSGT00940000163088; -.
DR   OMA; DPVNRTH; -.
DR   PRO; PR:A0A140LHF2; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; A0A140LHF2; protein.
DR   Bgee; ENSMUSG00000098590; Expressed in white adipose tissue.
DR   GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 5.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF48726; SSF48726; 4.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 4.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..776
FT                   /note="V-set and immunoglobulin domain-containing protein
FT                   10-like 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5008865835"
FT   TRANSMEM        713..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          32..140
FT                   /note="Ig-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          150..234
FT                   /note="Ig-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          242..324
FT                   /note="Ig-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          399..498
FT                   /note="Ig-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          500..592
FT                   /note="Ig-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          608..708
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   CARBOHYD        611
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        637
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        56..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        169..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        268..308
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        435..480
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        521..576
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   776 AA;  83270 MW;  8F29475B99292826 CRC64;
     MVGLSAHHRP LGCRLLILFC LLHPGASGQP YPTSNTAGEE ALSVQGVRGS SVELECRTGP
     APMAVLWSFT PLGSLVLQPV AVTSGASSKV ESGALALGVV SLRNSSLVIE ELREGARGHF
     LCQTLLVSGG QVHTAYLYLM LTVLVPVSKP RVQLNDPSPV EGVSVVATCA VREGTEPLTF
     SWHHHMPQGP GEVLVGLSEP RLQLDPVNRT HLGWYTCSVS NVVNQLKSDG AFLDVIYGPD
     KPVITVEPLG FSEDGFWASE REEVTLSCLA ASNPPSHYVW FRDDSQIHTG PTYIIASASR
     THTGLYTCLA HNRHLDTHTQ TTVQLIIYYP PEGQPSCAVL PTLGVVTLLC TWPGGFPNAQ
     LHWEGPQGIG PSASGNVTWS YTTTGLPNGS IFSCTGQHPT LAMPIFCRVT LWEPPGSPTC
     WTTATVGDQY IMLSCEWPGG EPPAMLSWLD RQQSLGDLGS SQAVHLLQAQ SDLAGREFTC
     QGSHPLTAPG SHCRLRLEVP QLTVAEPRVS VLEGEEAWLG CALQRGTPPA QLLWLGPQQQ
     QLEGSTPGFI LHPEGTHLRL QVRDADPAHH RGTYQCVARN ALGNSSQSVL LEVLSECKGF
     VCPCGYPTPP NVTISRLTYR RQRREVQLQW AIYGPGNLTG FLVQQRASVP SSEAGAWEVA
     ASDIEPESRD RRLGGLDPGV LYAFRILAMN HHTAGYPSEV KTPVDPAFSA YPAVLGAAGT
     GVVVALATSL LVFQYAARHP HTFPCTETAS TTSSSDPIQE SIDAPVNVTI TVTATP
 
 
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