MILL2_RAT
ID MILL2_RAT Reviewed; 372 AA.
AC A0A0G2K7V7; Q60I19;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=MHC class I-like protein MILL2 {ECO:0000305};
DE AltName: Full=MHC class I polypeptide-related sequence B {ECO:0000312|RGD:1564508};
DE AltName: Full=MHC class I-like located near the leukocyte receptor complex 2 {ECO:0000303|PubMed:15162429};
DE Flags: Precursor;
GN Name=Mill2 {ECO:0000303|PubMed:15162429};
GN Synonyms=Micb {ECO:0000312|RGD:1564508};
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|Proteomes:UP000002494};
RN [1] {ECO:0000312|EMBL:BAD54761.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=WkA/Hkm {ECO:0000312|EMBL:BAD54761.1};
RC TISSUE=Heart {ECO:0000312|EMBL:BAD54761.1};
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 -!- FUNCTION: Binds to heparan sulfate proteoglycans on the surface of
CC fibroblast cells. {ECO:0000250|UniProtKB:Q8HWE7}.
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: Ubiquitously expressed in neonatal and adult
CC tissues. {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; AB113961; BAD54761.1; -; mRNA.
DR EMBL; AC093995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001017468.1; NM_001017468.2.
DR AlphaFoldDB; A0A0G2K7V7; -.
DR SMR; A0A0G2K7V7; -.
DR GlyGen; A0A0G2K7V7; 3 sites.
DR PhosphoSitePlus; A0A0G2K7V7; -.
DR GeneID; 365212; -.
DR KEGG; rno:365212; -.
DR CTD; 4277; -.
DR RGD; 1564508; Micb.
DR VEuPathDB; HostDB:ENSRNOG00000057645; -.
DR OMA; DTINATC; -.
DR OrthoDB; 912212at2759; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000057645; Expressed in lung and 17 other tissues.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0046703; F:natural killer cell lectin-like receptor binding; ISO:RGD.
DR GO; GO:0046629; P:gamma-delta T cell activation; ISO:RGD.
DR GO; GO:0002429; P:immune response-activating cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:0050689; P:negative regulation of defense response to virus by host; ISO:RGD.
DR GO; GO:0009408; P:response to heat; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR GO; GO:0032526; P:response to retinoic acid; 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 Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 1.
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..350
FT /note="MHC class I-like protein MILL2"
FT /evidence="ECO:0000305"
FT /id="PRO_5002547003"
FT PROPEP 350..372
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000452208"
FT DOMAIN 192..302
FT /note="Ig-like C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 28..119
FT /note="Alpha-1"
FT /evidence="ECO:0000255"
FT REGION 120..210
FT /note="Alpha-2"
FT /evidence="ECO:0000255"
FT REGION 211..339
FT /note="Alpha-3"
FT /evidence="ECO:0000255"
FT REGION 308..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..348
FT /note="Connecting peptide"
FT /evidence="ECO:0000255"
FT LIPID 349
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250|UniProtKB:Q8HWE5"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..89
FT /evidence="ECO:0000250|UniProtKB:Q8HWE5"
FT DISULFID 129..191
FT /evidence="ECO:0000250|UniProtKB:Q8HWE5"
FT DISULFID 230..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 90..93
FT /note="TREA -> AREV (in Ref. 1; BAD54761)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="D -> E (in Ref. 1; BAD54761)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="D -> G (in Ref. 1; BAD54761)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="F -> FW (in Ref. 1; BAD54761)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="R -> H (in Ref. 1; BAD54761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 41001 MW; 45DA7F1DA95C7A81 CRC64;
MEASSGTAGP AVLLLILALL LTESQGSRSQ GTHTLRYDVT ACFLEGSEQT RLLVLIYVDD
ELFLRYNGDR RSAKPWACWI KGHGGDETCT REAENLPKEE ERLREMMADM INQKGHDKGP
YTLQATLDCE LQRNGSTRGF WHLGYEGRNL LTFDQKTLTW TMDVPFTQQK KTFEPRAPKA
DLVKTFLDET CPARLQRHLA SLSNVLPDTG SPVVIVTCRN YPVGRITLTC RAFNLSSRVA
TLLWLRDGKP VQQDVFGPGT ILPSGDGTYQ TWVSIRVLPG QEPQFACNLR HSNRTIMQTA
VSGESMGWPS ASWATRQEAE GPHRTHNDHV VDGGLVTGNA NKDSPDASSC ATASAISAFP
VVVLSVALPR AN
