MILL1_RAT
ID MILL1_RAT Reviewed; 404 AA.
AC Q60I18;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=MHC class I-like protein MILL1 {ECO:0000303|PubMed:15162429};
DE AltName: Full=MHC class I-like located near the leukocyte receptor complex 1 {ECO:0000303|PubMed:15162429};
DE Flags: Precursor;
GN Name=Mill1 {ECO:0000303|PubMed:15162429, ECO:0000312|RGD:1311714};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:BAD54762.1};
RN [1] {ECO:0000312|EMBL:BAD54762.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Brown Norway/SsN {ECO:0000312|EMBL:BAD54762.1};
RC TISSUE=Heart {ECO:0000312|EMBL:BAD54762.1};
RX PubMed=15162429; DOI=10.1002/eji.200424919;
RA Watanabe Y., Maruoka T., Walter L., Kasahara M.;
RT "Comparative genomics of the Mill family: a rapidly evolving MHC class I
RT gene family.";
RL Eur. J. Immunol. 34:1597-1607(2004).
RN [2] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
CC -!- SUBUNIT: Heterodimer with B2M. {ECO:0000250|UniProtKB:Q8HWE7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8HWE7};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8HWE7}.
CC -!- TISSUE SPECIFICITY: Detected in skin, esophagus, tongue, skin, muscle,
CC uterus, ovary, testis and epididymis. {ECO:0000269|PubMed:15162429}.
CC -!- DEVELOPMENTAL STAGE: In neonatal animals, highly expressed in skin.
CC {ECO:0000269|PubMed:15162429}.
CC -!- SIMILARITY: Belongs to the MHC class I family.
CC {ECO:0000255|RuleBase:RU004439}.
CC -!- CAUTION: Lacks key residues involved in peptide docking, suggesting
CC that this is a non-classical MHC class I protein which does not play a
CC role in antigen presentation. {ECO:0000305|PubMed:15162429}.
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DR EMBL; AB113962; BAD54762.1; -; mRNA.
DR EMBL; AC093995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001011931.1; NM_001011931.2.
DR RefSeq; XP_008757128.1; XM_008758906.2.
DR RefSeq; XP_008757129.1; XM_008758907.2.
DR AlphaFoldDB; Q60I18; -.
DR SMR; Q60I18; -.
DR STRING; 10116.ENSRNOP00000033032; -.
DR GlyGen; Q60I18; 4 sites.
DR PaxDb; Q60I18; -.
DR PRIDE; Q60I18; -.
DR Ensembl; ENSRNOT00000035286; ENSRNOP00000033032; ENSRNOG00000017699.
DR GeneID; 292671; -.
DR KEGG; rno:292671; -.
DR CTD; 266815; -.
DR RGD; 1311714; Mill1.
DR eggNOG; ENOG502RU00; Eukaryota.
DR GeneTree; ENSGT01040000240396; -.
DR InParanoid; Q60I18; -.
DR OMA; WVATRIS; -.
DR OrthoDB; 912212at2759; -.
DR PhylomeDB; Q60I18; -.
DR TreeFam; TF339076; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017699; Expressed in ovary and 12 other tissues.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0046703; F:natural killer cell lectin-like receptor binding; ISO:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0046629; P:gamma-delta T cell activation; ISO:RGD.
DR GO; GO:0002418; P:immune response to tumor cell; ISO:RGD.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:0032815; P:negative regulation of natural killer cell activation; ISO:RGD.
DR GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:0009408; P:response to heat; ISO:RGD.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR011161; MHC_I-like_Ag-recog.
DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR001039; MHC_I_a_a1/a2.
DR Pfam; PF00129; MHC_I; 1.
DR PRINTS; PR01638; MHCCLASSI.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..374
FT /note="MHC class I-like protein MILL1"
FT /evidence="ECO:0000305"
FT /id="PRO_5014106077"
FT PROPEP 375..404
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000452206"
FT DOMAIN 224..338
FT /note="Ig-like C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 59..150
FT /note="Alpha-1"
FT /evidence="ECO:0000255"
FT REGION 151..242
FT /note="Alpha-2"
FT /evidence="ECO:0000255"
FT REGION 243..342
FT /note="Alpha-3"
FT /evidence="ECO:0000255"
FT REGION 343..373
FT /note="Connecting peptide"
FT /evidence="ECO:0000255"
FT LIPID 374
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250|UniProtKB:Q8HWE7"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..223
FT /evidence="ECO:0000250|UniProtKB:Q8HWE5"
FT DISULFID 262..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 404 AA; 46422 MW; 238E6F5E04306EB7 CRC64;
MMLSRDLRAE AAVRLWIMFL LLEDLLGACA VGDYQRRVPS APNTDIRNTL EKPRVTTQEV
AGPHTLRYDL MALSLKLPEL PQVLIWRYFD DEPFLHYNES SNRTDSWEPR IKRHWRAMTW
ARETEDLQEM VEQLKRMLAE VTGQKGQDKG LHILQATLGC ELQRNGSTRG FWHLGYDGRN
LLTFDQKTLT WTMDMPFTQQ KKTFWEPRAP RADLVKTFLD DTCPAQLQRH LASLRSEPLD
TGSPMVIVTF RNYPLGRVTL TCRAFNLYPH MATRGTLAWL QDRKLVKQKA FEPGTILPSG
DRTYQIWVSI WVLPGQEPQF TCNLSYHGGN IEKRAVIVNT VSGEKTRQPS TSGVGGRVKK
SLWTTMTTAF MVTSWTRKTG GDSTLLLLWW LLFFSTVLAV LTLV
