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   18-JUN-2025, entry version 150.
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_013552.3. [Q00547-1]
DR   AlphaFoldDB; Q00547; -.
DR   SMR; Q00547; -.
DR   BioGRID; 200343; 2.
DR   DIP; DIP-46343N; -.
DR   FunCoup; Q00547; 761.
DR   IntAct; Q00547; 1.
DR   STRING; 10090.ENSMUSP00000020579; -.
DR   GlyCosmos; Q00547; 9 sites, No reported glycans.
DR   GlyGen; Q00547; 10 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q00547; -.
DR   PhosphoSitePlus; Q00547; -.
DR   jPOST; Q00547; -.
DR   PaxDb; 10090-ENSMUSP00000020579; -.
DR   PeptideAtlas; Q00547; -.
DR   ProteomicsDB; 267055; -. [Q00547-1]
DR   ProteomicsDB; 267056; -. [Q00547-2]
DR   Pumba; Q00547; -.
DR   Antibodypedia; 39622; 463 antibodies from 41 providers.
DR   DNASU; 15366; -.
DR   Ensembl; ENSMUST00000020579.9; ENSMUSP00000020579.8; ENSMUSG00000020330.17. [Q00547-1]
DR   GeneID; 15366; -.
DR   KEGG; mmu:15366; -.
DR   UCSC; uc007ils.2; mouse. [Q00547-1]
DR   AGR; MGI:104667; -.
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; NEHIGCA; -.
DR   OrthoDB; 419631at2759; -.
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 78 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 195 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0038024; F:cargo receptor activity; IDA:MGI.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0030214; P:hyaluronan catabolic process; IDA:MGI.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IDA:MGI.
DR   InterPro; IPR031794; HMMR_C.
DR   InterPro; IPR026203; IHABP.
DR   PANTHER; PTHR18956; HYALURONAN MEDIATED MOTILITY RECEPTOR; 1.
DR   PANTHER; PTHR18956:SF6; HYALURONAN MEDIATED MOTILITY RECEPTOR; 1.
DR   Pfam; PF15908; HMMR_C; 1.
DR   Pfam; PF15905; HMMR_N; 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        74..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
//