SKIT1_MOUSE
ID SKIT1_MOUSE Reviewed; 364 AA.
AC A7TZE6; A7TZE7; A7XUW2; A7XUW8; A7XUX1; A9XK90;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Selection and upkeep of intraepithelial T-cells protein 1;
DE Short=Skint-1;
DE AltName: Full=Immunoglobulin-like and transmembrane domain-containing protein expressed in skin and thymus protein 1;
DE Flags: Precursor;
GN Name=Skint1;
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 [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, TISSUE
RP SPECIFICITY, POLYMORPHISM, AND VARIANT 324-GLU--ASN-364 DEL.
RC STRAIN=C57BL/6J, FVB/NJ, and FVB/NTac;
RX PubMed=18408721; DOI=10.1038/ng.108;
RA Boyden L.M., Lewis J.M., Barbee S.D., Bas A., Girardi M., Hayday A.C.,
RA Tigelaar R.E., Lifton R.P.;
RT "Skint1, the prototype of a newly identified immunoglobulin superfamily
RT gene cluster, positively selects epidermal gammadelta T cells.";
RL Nat. Genet. 40:656-662(2008).
RN [2]
RP GENE EVOLUTION.
RX PubMed=25830554; DOI=10.1371/journal.pone.0123258;
RA Mohamed R.H., Sutoh Y., Itoh Y., Otsuka N., Miyatake Y., Ogasawara K.,
RA Kasahara M.;
RT "The SKINT1-like gene is inactivated in hominoids but not in all primate
RT species: Implications for the origin of dendritic epidermal T cells.";
RL PLoS ONE 10:E0123258-E0123258(2015).
CC -!- FUNCTION: May act by engaging a cell surface molecule on immature T-
CC cells in the embryonic thymus. Plays a central role in mediating key
CC epithelial-immune interactions by being involved in the selection of
CC Vgamma5(+)Vdelta1(+) T-cells, which constitute 90% of epidermal
CC gammadelta T-cells. {ECO:0000269|PubMed:18408721}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=A;
CC IsoId=A7TZE6-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=A7TZE6-2; Sequence=VSP_034875, VSP_034876;
CC Name=3; Synonyms=C;
CC IsoId=A7TZE6-3; Sequence=VSP_034873, VSP_034874;
CC Name=4; Synonyms=D;
CC IsoId=A7TZE6-4; Sequence=VSP_034871, VSP_034872;
CC -!- TISSUE SPECIFICITY: Expressed in skin and thymus.
CC {ECO:0000269|PubMed:18408721}.
CC -!- POLYMORPHISM: The strain FVB/NTac displays a selective deficiency for
CC epidermal Vgamma5(+)Vdelta1(+) T-cells due to a mutation that creates
CC premature codon stop at position 324. {ECO:0000269|PubMed:18408721}.
CC -!- MISCELLANEOUS: Encoded by one of the 11 copies of Skint genes clustered
CC in the D1 region of the chromosome 4.
CC -!- MISCELLANEOUS: Humans and chimpanzees have a SKINT1-like (SKINT1L) gene
CC with multiple inactivating mutations. All hominoid species have a
CC common inactivating mutation, but that Old World monkeys such as olive
CC baboons, green monkeys, cynomolgus macaques and rhesus macaques have
CC apparently functional SKINT1L sequences, indicating that SKINT1L is
CC inactivated in a common ancestor of hominoids.
CC {ECO:0000305|PubMed:25830554}.
CC -!- SIMILARITY: Belongs to the SKINT family. {ECO:0000305}.
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DR EMBL; EF494889; ABS30711.1; -; mRNA.
DR EMBL; EF494890; ABS30712.1; -; mRNA.
DR EMBL; EF494891; ABS30713.1; -; mRNA.
DR EMBL; EU099296; ABU87894.1; -; mRNA.
DR EMBL; EU099297; ABU87895.1; -; mRNA.
DR EMBL; EU099298; ABU87896.1; -; mRNA.
DR CCDS; CCDS51267.1; -. [A7TZE6-1]
DR RefSeq; NP_001096132.1; NM_001102662.1. [A7TZE6-1]
DR PDB; 2N4I; NMR; -; A=24-141.
DR PDBsum; 2N4I; -.
DR AlphaFoldDB; A7TZE6; -.
DR SMR; A7TZE6; -.
DR DIP; DIP-59617N; -.
DR STRING; 10090.ENSMUSP00000124737; -.
DR GlyGen; A7TZE6; 1 site.
DR PaxDb; A7TZE6; -.
DR PRIDE; A7TZE6; -.
DR Ensembl; ENSMUST00000117379; ENSMUSP00000124545; ENSMUSG00000089773. [A7TZE6-3]
DR Ensembl; ENSMUST00000161389; ENSMUSP00000125313; ENSMUSG00000089773. [A7TZE6-2]
DR Ensembl; ENSMUST00000162158; ENSMUSP00000124737; ENSMUSG00000089773. [A7TZE6-1]
DR Ensembl; ENSMUST00000162885; ENSMUSP00000125625; ENSMUSG00000089773. [A7TZE6-4]
DR GeneID; 639781; -.
DR KEGG; mmu:639781; -.
DR UCSC; uc008udq.1; mouse. [A7TZE6-1]
DR UCSC; uc009vcw.1; mouse. [A7TZE6-4]
DR UCSC; uc012dip.1; mouse. [A7TZE6-2]
DR CTD; 639781; -.
DR MGI; MGI:3649627; Skint1.
DR VEuPathDB; HostDB:ENSMUSG00000089773; -.
DR eggNOG; ENOG502SEQH; Eukaryota.
DR GeneTree; ENSGT00940000162562; -.
DR HOGENOM; CLU_013137_10_4_1; -.
DR InParanoid; A7TZE6; -.
DR OMA; WVEDISV; -.
DR OrthoDB; 812118at2759; -.
DR PhylomeDB; A7TZE6; -.
DR TreeFam; TF331083; -.
DR BioGRID-ORCS; 639781; 1 hit in 72 CRISPR screens.
DR PRO; PR:A7TZE6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A7TZE6; protein.
DR Bgee; ENSMUSG00000089773; Expressed in zone of skin and 8 other tissues.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISM:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; IDA:MGI.
DR GO; GO:0042492; P:gamma-delta T cell differentiation; IDA:MGI.
DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IDA:MGI.
DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IDA:MGI.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IDA:MGI.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IMP:MGI.
DR GO; GO:0045059; P:positive thymic T cell selection; IDA:MGI.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0030217; P:T cell differentiation; IDA:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
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; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..364
FT /note="Selection and upkeep of intraepithelial T-cells
FT protein 1"
FT /id="PRO_5000270102"
FT TOPO_DOM 24..246
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..325
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..141
FT /note="Ig-like V-type"
FT DOMAIN 142..228
FT /note="Ig-like C1-type"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 142..163
FT /note="AINLQVQIHVHPPNTKGVIVEC -> GGNGSFRGFYESTFFNSSGSER (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:18408721"
FT /id="VSP_034871"
FT VAR_SEQ 164..364
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:18408721"
FT /id="VSP_034872"
FT VAR_SEQ 236..255
FT /note="DAFFSWNRIWKMILGIILSM -> VVCYIMSIKVRMPRGSRGGN (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:18408721"
FT /id="VSP_034873"
FT VAR_SEQ 256..364
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18408721"
FT /id="VSP_034874"
FT VAR_SEQ 273..289
FT /note="VCKWKWDAPWIKGLLIM -> GTYATWEQGRELVLHKP (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:18408721"
FT /id="VSP_034875"
FT VAR_SEQ 290..364
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18408721"
FT /id="VSP_034876"
FT VARIANT 324..364
FT /note="Missing (in strain: FVB/NTac)"
FT /evidence="ECO:0000269|PubMed:18408721"
FT CONFLICT 22
FT /note="T -> I (in Ref. 1; ABS30712/ABS30713)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="P -> Q (in Ref. 1; ABS30712/ABS30713)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="A -> V (in Ref. 1; ABS30712/ABS30713)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="R -> Q (in Ref. 1; ABS30712/ABS30713)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="A -> T (in Ref. 1; ABS30712/ABS30713)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="I -> M (in Ref. 1; ABS30712/ABS30713)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="K -> T (in Ref. 1; ABS30712/ABS30713)"
FT /evidence="ECO:0000305"
FT CONFLICT 250..252
FT /note="GII -> SIM (in Ref. 1; ABS30712/ABS30713)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="H -> Y (in Ref. 1; ABS30712/ABS30713)"
FT /evidence="ECO:0000305"
FT CONFLICT 275..276
FT /note="KW -> RC (in Ref. 1; ABS30712/ABS30713)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="T -> I (in Ref. 1; ABS30712/ABS30713)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="M -> V (in Ref. 1; ABS30712/ABS30713)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="M -> K (in Ref. 1; ABS30712/ABS30713)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="V -> I (in Ref. 1; ABS30712/ABS30713)"
FT /evidence="ECO:0000305"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2N4I"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2N4I"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:2N4I"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:2N4I"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2N4I"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:2N4I"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:2N4I"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:2N4I"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:2N4I"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:2N4I"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:2N4I"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:2N4I"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:2N4I"
SQ SEQUENCE 364 AA; 41792 MW; BBAA9DD4CAD96DF5 CRC64;
MGSTGLCFYG HCIVMFLLQM VTASSEPFIV NGLEGPVLAS LGGNLELSCQ LSPPQQAQHM
EIRWFRNLYT EPVHLYRDGK DMFGEIISKY VERTELLKDG IGEGKVTLRI FNVTVDDDGS
YHCVFKDGDF YEEHITEVKI TAINLQVQIH VHPPNTKGVI VECHSGGWFP RPLMQWRDRR
GEVIPAASKS HSQGRDKLFN MKISLLISES FFQKVICCLQ NPLTGQEERT SVILSDAFFS
WNRIWKMILG IILSMMVVSI FVFSCLLHHE HKVCKWKWDA PWIKGLLIMT SSMVTVVLVM
VYLHMKQRVP VSDVHFELDT LWVEDISVIL CSLMVPATML VSYTYFRLKD WCQHNHAQRV
FTSN
