MILL1_MOUSE
ID MILL1_MOUSE Reviewed; 395 AA.
AC Q8HWE7; Q8HWA4; Q8HWA5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=MHC class I-like protein MILL1 {ECO:0000305};
DE AltName: Full=MHC class I-like located near the leukocyte receptor complex 1 {ECO:0000303|PubMed:12370446};
DE Flags: Precursor;
GN Name=Mill1 {ECO:0000303|PubMed:12370446};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:BAC21669.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:BAC21669.1};
RC TISSUE=Skin {ECO:0000312|EMBL:BAC21669.1};
RX PubMed=12370446; DOI=10.1073/pnas.212375299;
RA Kasahara M., Watanabe Y., Sumasu M., Nagata T.;
RT "A family of MHC class I-like genes located in the vicinity of the mouse
RT leukocyte receptor complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13687-13692(2002).
RN [2] {ECO:0000312|EMBL:BAC26240.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26240.1};
RC TISSUE=Skin {ECO:0000312|EMBL:BAC26240.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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).
RN [4] {ECO:0000312|EMBL:AAI10548.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5] {ECO:0000305}
RP SUBUNIT, INTERACTION WITH B2M, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP GLYCOSYLATION, AND GPI-ANCHOR AT SER-369.
RX PubMed=16920948; DOI=10.4049/jimmunol.177.5.3108;
RA Kajikawa M., Baba T., Tomaru U., Watanabe Y., Koganei S.,
RA Tsuji-Kawahara S., Matsumoto N., Yamamoto K., Miyazawa M., Maenaka K.,
RA Ishizu A., Kasahara M.;
RT "MHC class I-like MILL molecules are beta2-microglobulin-associated, GPI-
RT anchored glycoproteins that do not require TAP for cell surface
RT expression.";
RL J. Immunol. 177:3108-3115(2006).
CC -!- SUBUNIT: Heterodimer with B2M. {ECO:0000269|PubMed:16920948}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16920948};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:16920948}.
CC -!- TISSUE SPECIFICITY: Expressed in stomach, intestine, uterus, skeletal
CC muscle and heart. {ECO:0000269|PubMed:12370446}.
CC -!- DEVELOPMENTAL STAGE: In neonatal animals, highly expressed in skin
CC where it localizes to a region of the inner root sheath of hair
CC follicles (at protein level) (PubMed:12370446, PubMed:16920948). Also
CC expressed in thymic medullary epithelial cells (at protein level)
CC (PubMed:12370446, PubMed:16920948). Detected in skeletal muscle, eyes,
CC and submandibular glands (PubMed:12370446).
CC {ECO:0000269|PubMed:12370446, ECO:0000269|PubMed:16920948}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16920948}.
CC -!- SIMILARITY: Belongs to the MHC class I family.
CC {ECO:0000255|RuleBase:RU004439}.
CC -!- CAUTION: Lacks key residues involved in peptide docking and also does
CC not require TAP (transporter involved in antigen processing) for cell
CC surface expression, suggesting that this is a non-classical MHC class I
CC protein which does not play a role in antigen presentation.
CC {ECO:0000305|PubMed:12370446, ECO:0000305|PubMed:16920948}.
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DR EMBL; AK029010; BAC26240.1; -; mRNA.
DR EMBL; AK030695; BAC27084.1; -; mRNA.
DR EMBL; AC151983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110547; AAI10548.1; -; mRNA.
DR EMBL; BC110548; AAI10549.1; -; mRNA.
DR EMBL; AB086265; BAC21669.1; -; mRNA.
DR CCDS; CCDS20868.1; -.
DR RefSeq; NP_715630.3; NM_153749.4.
DR AlphaFoldDB; Q8HWE7; -.
DR SMR; Q8HWE7; -.
DR STRING; 10090.ENSMUSP00000069083; -.
DR GlyGen; Q8HWE7; 3 sites.
DR PaxDb; Q8HWE7; -.
DR PRIDE; Q8HWE7; -.
DR ProteomicsDB; 328731; -.
DR DNASU; 266815; -.
DR Ensembl; ENSMUST00000066780; ENSMUSP00000069083; ENSMUSG00000054005.
DR GeneID; 266815; -.
DR KEGG; mmu:266815; -.
DR UCSC; uc009fjh.1; mouse.
DR CTD; 266815; -.
DR MGI; MGI:2179988; Mill1.
DR VEuPathDB; HostDB:ENSMUSG00000054005; -.
DR eggNOG; ENOG502RU00; Eukaryota.
DR GeneTree; ENSGT01040000240396; -.
DR HOGENOM; CLU_047501_4_0_1; -.
DR InParanoid; Q8HWE7; -.
DR OMA; WVATRIS; -.
DR OrthoDB; 912212at2759; -.
DR PhylomeDB; Q8HWE7; -.
DR TreeFam; TF339076; -.
DR BioGRID-ORCS; 266815; 1 hit in 74 CRISPR screens.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8HWE7; protein.
DR Bgee; ENSMUSG00000054005; Expressed in zone of skin and 6 other tissues.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; PF07654; C1-set; 1.
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 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..369
FT /note="MHC class I-like protein MILL1"
FT /evidence="ECO:0000255"
FT /id="PRO_5015099152"
FT PROPEP 370..395
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:16920948"
FT /id="PRO_0000452205"
FT DOMAIN 242..333
FT /note="Ig-like C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 57..148
FT /note="Alpha-1"
FT /evidence="ECO:0000255"
FT REGION 149..240
FT /note="Alpha-2"
FT /evidence="ECO:0000255"
FT REGION 241..337
FT /note="Alpha-3"
FT /evidence="ECO:0000255"
FT REGION 332..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..368
FT /note="Connecting peptide"
FT /evidence="ECO:0000255"
FT LIPID 369
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000305|PubMed:16920948"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 158..221
FT /evidence="ECO:0000250|UniProtKB:Q8HWE5"
FT DISULFID 260..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 58
FT /note="V -> L (in Ref. 2; BAC27084)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="F -> L (in Ref. 2; BAC27084)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="T -> A (in Ref. 2; BAC27084)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="M -> L (in Ref. 2; BAC26240)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 44745 MW; FA076D1DB7060364 CRC64;
MLLSRNLRAL AAIHLWIVYL LLEDLLGTCA EGDNQRLVAS APYQDIEITL EKPRVQAVAE
PHTLRYDLMA LSLEVPGLPQ FLTLRYFDDE PFLPYKKNSS ITDSQEPRIK DHLRAETWGR
ETDDLQEEEE QLKGMLAEIT AQNGQNTDLH ILQATFGCEL QRNGSTRGFW KLGYDGQNFL
TFDQKTLTWT VDGPSTQKNK TFWKTRAPRA DLVKTFLDDI CPAQLQRYLA SLRNGLLNTG
FPKVIVTFRN YPVGRITLTC RAFRLYTRVA TLTWLQYRKP VQQKTFGSET ILPSGDGTYQ
AWVSIRVLPG QESQFSCNLK HGNHNINEPA ATEAPVYGAR REQPPTSGVG SRVGKSLWSA
MTTALVVISW TLSQKLMGPL LWFCSGGFCS FLQCW
