VSXL2_HUMAN
ID VSXL2_HUMAN Reviewed; 767 AA.
AC P0DP72;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2017, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=V-set and immunoglobulin domain-containing protein 10-like 2 {ECO:0000312|HGNC:HGNC:27879};
DE Flags: Precursor;
GN Name=VSIG10L2 {ECO:0000312|HGNC:HGNC:27879};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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DR EMBL; AP000842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0DP72; -.
DR IntAct; P0DP72; 2.
DR GlyGen; P0DP72; 3 sites.
DR BioMuta; VSIG10L2; -.
DR PeptideAtlas; P0DP72; -.
DR PRIDE; P0DP72; -.
DR Ensembl; ENST00000638636.2; ENSP00000491467.1; ENSG00000283703.3.
DR GeneCards; VSIG10L2; -.
DR HGNC; HGNC:27879; VSIG10L2.
DR HPA; ENSG00000283703; Tissue enriched (skin).
DR neXtProt; NX_P0DP72; -.
DR VEuPathDB; HostDB:ENSG00000283703; -.
DR GeneTree; ENSGT00940000163088; -.
DR OMA; DPVNRTH; -.
DR Pharos; P0DP72; Tdark.
DR PRO; PR:P0DP72; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P0DP72; protein.
DR Bgee; ENSG00000283703; Expressed in skin of abdomen and 101 other tissues.
DR ExpressionAtlas; P0DP72; baseline and differential.
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; -; 4.
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 Pfam; PF00041; fn3; 1.
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..767
FT /note="V-set and immunoglobulin domain-containing protein
FT 10-like 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000440969"
FT TRANSMEM 704..724
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 34..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..499
FT /note="Ig-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 501..593
FT /note="Ig-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 599..699
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 735..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
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..481
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 522..577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 767 AA; 81629 MW; ECFC0378D37468B6 CRC64;
MVGQRAQHSP VSLLLLIHLC LLHLRASGQP HPTPEAPVEE VVSVQGVRGG SVELACGSGP
APLLVLWSFT PLGSLVPRPV AVTDGAMSKV EAIASALGVV SLRNSSLVLG ELHEGARGHF
LCQVLHVAGG QLHAAYSHLT LAVLVPVSKP QVRLSNPSPV EGASVVATCA VREGTEPVTF
AWQHRAPRGL GEALVGVTEP LFQLDPVNRT HLGWYMCSAS NSVNRLSSDG AFLDVIYGPD
KPVITMEPLG LTEEGFWASE REEVTLSCLA ASNPPSHYVW LRDHTQVHTG PTYVIARAGR
VHTGLYTCLA RNSYLDTRTQ TTVQLTIYYP PEGQPSCAVH PSPEAVTLLC AWPGGLPPAQ
LQWEGPQGPG PTAPSNVTWS HAAAQLPSGS VFTCTGQHPA LAPPALCTVM LWEPLGRPTC
WSTATMGDQF IMLSCEWPGG EPPATLGWLD EQQQPLGGSS SSMAVHLLQA QEDLAGREFT
CRGTHLLRTP DPHCHLQLEA PQLDVAEPRV SVLEGGEAWL ECSLRGGTPP AQLLWLGPQQ
QKVDPGTSGF MLHPEGAQLR LGIYDADPAH HRGTYQCVAR NAVGNSSQSV LLEVLRYPAP
PNVTISRLTY GRHRREVQLQ WAILGPGNLT GFLVQRKASA LGPGAGAWET AASDIEPESR
GRRLGGLDPG VLYAFRILAL NHHTAGHPSE VKIPADPPFS AYPAVLGAAG TGMVVATVAS
LLVFQYAARH PETFPRLETP TTTPGLDPAQ ETTDSPVNVT ITVTATP
