HMMR_MOUSE
ID HMMR_MOUSE Reviewed; 794 AA.
AC Q00547; Q5NC88;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Hyaluronan mediated motility receptor;
DE AltName: Full=Intracellular hyaluronic acid-binding protein;
DE AltName: Full=Receptor for hyaluronan-mediated motility;
DE AltName: CD_antigen=CD168;
GN Name=Hmmr; Synonyms=Ihabp, Rhamm;
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], AND SUBCELLULAR LOCATION.
RC TISSUE=Lung;
RX PubMed=9601097; DOI=10.1242/jcs.111.12.1673;
RA Hofmann M., Fieber C., Assmann V., Goettlicher M., Sleeman J., Plug R.,
RA Howells N., von Stein O., Ponta H., Herrlich P.;
RT "Identification of IHABP, a 95 kDa intracellular hyaluronate binding
RT protein.";
RL J. Cell Sci. 111:1673-1684(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhao Y., Zhang S., Turley E.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-183, AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=9889313; DOI=10.1016/s0378-1119(98)00566-6;
RA Fieber C., Plug R., Sleeman J., Dall P., Ponta H., Hofmann M.;
RT "Characterization of the murine gene encoding the intracellular hyaluronan
RT receptor IHABP.";
RL Gene 226:41-50(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 164-794, AND ALTERNATIVE SPLICING.
RC STRAIN=BALB/cJ; TISSUE=Fibroblast;
RX PubMed=7590272; DOI=10.1016/0378-1119(95)00398-p;
RA Entwistle J., Zhang S., Yang B., Wong C., Li Q., Hall C.L., Jingbo A.,
RA Mowat M., Greenberg A.H., Turley E.A.;
RT "Characterization of the murine gene encoding the hyaluronan receptor
RT RHAMM.";
RL Gene 163:233-238(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 318-794, SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=BALB/cJ;
RX PubMed=1376732; DOI=10.1083/jcb.117.6.1343;
RA Hardwick C., Hoare K., Owens R., Hohn H.P., Hook M., Moore D., Cripps V.,
RA Austen L., Nance D.M., Turley E.A.;
RT "Molecular cloning of a novel hyaluronan receptor that mediates tumor cell
RT motility.";
RL J. Cell Biol. 117:1343-1350(1992).
RN [8]
RP ERRATUM OF PUBMED:1376732.
RX PubMed=1639856; DOI=10.1083/jcb.118.3.753;
RA Hardwick C., Hoare K., Owens R., Hohn H.P., Hook M., Moore D., Cripps V.,
RA Austen L., Nance D.M., Turley E.A.;
RL J. Cell Biol. 118:753-753(1992).
RN [9]
RP CHARACTERIZATION.
RX PubMed=7518470; DOI=10.1083/jcb.126.2.575;
RA Hall C.L., Wang C., Lange L.A., Turley E.A.;
RT "Hyaluronan and the hyaluronan receptor RHAMM promote focal adhesion
RT turnover and transient tyrosine kinase activity.";
RL J. Cell Biol. 126:575-588(1994).
RN [10]
RP ERK REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=9556628; DOI=10.1074/jbc.273.18.11342;
RA Zhang S., Chang M.C., Zylka D., Turley S., Harrison R., Turley E.A.;
RT "The hyaluronan receptor RHAMM regulates extracellular-regulated kinase.";
RL J. Biol. Chem. 273:11342-11348(1998).
RN [11]
RP REVIEW.
RX PubMed=9845361; DOI=10.1016/s0092-8674(00)81628-1;
RA Hofmann M., Assmann V., Fieber C., Sleeman J.P., Moll J., Ponta H.,
RA Hart I.R., Herrlich P.;
RT "Problems with RHAMM: a new link between surface adhesion and
RT oncogenesis?";
RL Cell 95:591-592(1998).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION.
RX PubMed=22666460; DOI=10.1371/journal.pone.0038130;
RA Liu X.F., Bera T.K., Kahue C., Escobar T., Fei Z., Raciti G.A., Pastan I.;
RT "ANKRD26 and its interacting partners TRIO, GPS2, HMMR and DIPA regulate
RT adipogenesis in 3T3-L1 cells.";
RL PLoS ONE 7:E38130-E38130(2012).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=31338967; DOI=10.15252/embr.201847495;
RA Fulcher L.J., He Z., Mei L., Macartney T.J., Wood N.T., Prescott A.R.,
RA Whigham A.J., Varghese J., Gourlay R., Ball G., Clarke R., Campbell D.G.,
RA Maxwell C.A., Sapkota G.P.;
RT "FAM83D directs protein kinase CK1alpha to the mitotic spindle for proper
RT spindle positioning.";
RL EMBO Rep. 20:e47495-e47495(2019).
CC -!- FUNCTION: Receptor for hyaluronic acid (HA) (PubMed:1376732). Involved
CC in cell motility (PubMed:1376732). When hyaluronan binds to HMMR, the
CC phosphorylation of a number of proteins, including the PTK2/FAK1
CC occurs. May also be involved in cellular transformation and metastasis
CC formation, and in regulating extracellular-regulated kinase (ERK)
CC activity. May act as a regulator of adipogenesis (PubMed:22666460).
CC {ECO:0000269|PubMed:1376732, ECO:0000269|PubMed:22666460}.
CC -!- SUBUNIT: Interacts with ANKRD26 (By similarity). Interacts with DYNLL1
CC (By similarity). Interacts with FAM83D/CHICA (By similarity).
CC {ECO:0000250|UniProtKB:O75330}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:1376732,
CC ECO:0000269|PubMed:9556628}. Cytoplasm {ECO:0000269|PubMed:9556628,
CC ECO:0000269|PubMed:9601097}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:31338967}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=RHAMM1V4;
CC IsoId=Q00547-1; Sequence=Displayed;
CC Name=RHAMM1;
CC IsoId=Q00547-2; Sequence=VSP_004287;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9889313}.
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DR EMBL; AF031932; AAC12655.1; -; mRNA.
DR EMBL; AF079222; AAD08670.1; -; mRNA.
DR EMBL; AL646055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466609; EDL32330.1; -; Genomic_DNA.
DR EMBL; AJ005919; CAA06768.1; -; Genomic_DNA.
DR EMBL; AJ005920; CAA06768.1; JOINED; Genomic_DNA.
DR EMBL; AJ005921; CAA06768.1; JOINED; Genomic_DNA.
DR EMBL; AJ005922; CAA06768.1; JOINED; Genomic_DNA.
DR EMBL; AJ005923; CAA06768.1; JOINED; Genomic_DNA.
DR EMBL; AJ005924; CAA06768.1; JOINED; Genomic_DNA.
DR EMBL; X64550; CAA45849.1; -; mRNA.
DR EMBL; X64550; CAA45848.1; -; mRNA.
DR CCDS; CCDS24548.1; -. [Q00547-1]
DR PIR; JC4298; JC4298.
DR RefSeq; NP_038580.2; NM_013552.2. [Q00547-1]
DR AlphaFoldDB; Q00547; -.
DR SMR; Q00547; -.
DR BioGRID; 200343; 1.
DR DIP; DIP-46343N; -.
DR IntAct; Q00547; 1.
DR STRING; 10090.ENSMUSP00000020579; -.
DR GlyGen; Q00547; 9 sites.
DR iPTMnet; Q00547; -.
DR PhosphoSitePlus; Q00547; -.
DR EPD; Q00547; -.
DR MaxQB; Q00547; -.
DR PaxDb; Q00547; -.
DR PeptideAtlas; Q00547; -.
DR PRIDE; Q00547; -.
DR ProteomicsDB; 267055; -. [Q00547-1]
DR ProteomicsDB; 267056; -. [Q00547-2]
DR Antibodypedia; 39622; 472 antibodies from 41 providers.
DR DNASU; 15366; -.
DR Ensembl; ENSMUST00000020579; ENSMUSP00000020579; ENSMUSG00000020330. [Q00547-1]
DR GeneID; 15366; -.
DR KEGG; mmu:15366; -.
DR UCSC; uc007ils.2; mouse. [Q00547-1]
DR CTD; 3161; -.
DR MGI; MGI:104667; Hmmr.
DR VEuPathDB; HostDB:ENSMUSG00000020330; -.
DR eggNOG; ENOG502QQJM; Eukaryota.
DR GeneTree; ENSGT00390000007135; -.
DR HOGENOM; CLU_009698_0_0_1; -.
DR InParanoid; Q00547; -.
DR OMA; KEHKCVE; -.
DR PhylomeDB; Q00547; -.
DR TreeFam; TF333963; -.
DR Reactome; R-MMU-2160916; Hyaluronan uptake and degradation.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 15366; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Hmmr; mouse.
DR PRO; PR:Q00547; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q00547; protein.
DR Bgee; ENSMUSG00000020330; Expressed in optic fissure and 192 other tissues.
DR Genevisible; Q00547; MM.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR InterPro; IPR031794; HMMR_C.
DR InterPro; IPR026203; IHABP.
DR PANTHER; PTHR18956; PTHR18956; 3.
DR Pfam; PF15908; HMMR_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Glycoprotein;
KW Hyaluronic acid; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..794
FT /note="Hyaluronan mediated motility receptor"
FT /id="PRO_0000084008"
FT REPEAT 442..462
FT /note="1"
FT REPEAT 463..483
FT /note="2"
FT REPEAT 484..504
FT /note="3"
FT REPEAT 505..525
FT /note="4"
FT REPEAT 526..546
FT /note="5"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..630
FT /note="Required for interaction with FAM83D"
FT /evidence="ECO:0000250|UniProtKB:O75330"
FT REGION 442..546
FT /note="5 X 21 AA tandem repeats"
FT REGION 719..729
FT /note="Hyaluronic acid-binding"
FT /evidence="ECO:0000255"
FT REGION 741..750
FT /note="Hyaluronic acid-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 32..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75330"
FT MOD_RES 784
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75330"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 218..242
FT /note="Missing (in isoform RHAMM1)"
FT /evidence="ECO:0000305"
FT /id="VSP_004287"
FT CONFLICT 19
FT /note="P -> Q (in Ref. 5; CAA06768)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="N -> S (in Ref. 1; AAC12655 and 5; CAA06768)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="K -> T (in Ref. 2; AAD08670)"
FT /evidence="ECO:0000305"
FT CONFLICT 89..91
FT /note="EKE -> QKH (in Ref. 2; AAD08670)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="A -> V (in Ref. 5; CAA06768)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="T -> R (in Ref. 1; AAC12655, 2; AAD08670, 6;
FT CAA45849 and 7; CAA45848)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="T -> S (in Ref. 1; AAC12655, 6; CAA45849 and 7;
FT CAA45848)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="E -> D (in Ref. 2; AAD08670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 794 AA; 91785 MW; 58482E8587E4F4DA CRC64;
MSFPKAPLKR FNDPSGCAPS PGAYDVKTSE ATKGPVSFQK SQRFKNQRES QQNLNIDKDT
TLLASAKKAK KSVSKKDSQK NDKDVKRLEK EIRALLQERG TQDKRIQDME SELEKTEAKL
NAAVREKTSL SASNASLEKR LTELTRANEL LKAKFSEDGH QKNMRALSLE LMKLRNKRET
KMRSMMVKQE GMELKLQATQ KDLTESKGKI VQLEGKLVSI EKEKIDEKCE TEKLLEYIQE
ISCASDQVEK CKVDIAQLEE DLKEKDREIL SLKQSLEENI TFSKQIEDLT VKCQLLETER
DNLVSKDRER AETLSAEMQI LTERLALERQ EYEKLQQKEL QSQSLLQQEK ELSARLQQQL
CSFQEEMTSE KNVFKEELKL ALAELDAVQQ KEEQSERLVK QLEEETKSTA EQLTRLDNLL
REKEVELEKH IAAHAQAILI AQEKYNDTAQ SLRDVTAQLE SVQEKYNDTA QSLRDVTAQL
ESEQEKYNDT AQSLRDVTAQ LESEQEKYND TAQSLRDVTA QLESVQEKYN DTAQSLRDVT
AQLESYKSST LKEIEDLKLE NLTLQEKVAM AEKSVEDVQQ QILTAESTNQ EYARMVQDLQ
NRSTLKEEEI KEITSSFLEK ITDLKNQLRQ QDEDFRKQLE EKGKRTAEKE NVMTELTMEI
NKWRLLYEEL YEKTKPFQQQ LDAFEAEKQA LLNEHGATQE QLNKIRDSYA QLLGHQNLKQ
KIKHVVKLKD ENSQLKSEVS KLRSQLVKRK QNELRLQGEL DKALGIRHFD PSKAFCHASK
ENFTPLKEGN PNCC
