ID   HMMR_RAT                Reviewed;         498 AA.
AC   P97779;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 84.
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   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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Vascular smooth muscle;
RA   Savani R.C., Hou G.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for hyaluronic acid (HA) (By similarity). Involved
CC       in cell motility (By similarity). 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 (By similarity). May act as a regulator of adipogenisis (By
CC       similarity). {ECO:0000250|UniProtKB:Q00547}.
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:0000250|UniProtKB:Q00547}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q00547}. Cytoplasm, cytoskeleton,
CC       spindle {ECO:0000250|UniProtKB:Q00547}.
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DR   EMBL; U87983; AAB47997.1; -; mRNA.
DR   AlphaFoldDB; P97779; -.
DR   SMR; P97779; -.
DR   IntAct; P97779; 1.
DR   MINT; P97779; -.
DR   GlyGen; P97779; 3 sites.
DR   PhosphoSitePlus; P97779; -.
DR   jPOST; P97779; -.
DR   PRIDE; P97779; -.
DR   UCSC; RGD:2805; rat.
DR   RGD; 2805; Hmmr.
DR   InParanoid; P97779; -.
DR   Reactome; R-RNO-2160916; Hyaluronan uptake and degradation.
DR   Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR   PRO; PR:P97779; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR   GO; GO:0005540; F:hyaluronic acid binding; TAS:RGD.
DR   GO; GO:0007267; P:cell-cell signaling; NAS:RGD.
DR   GO; GO:0007010; P:cytoskeleton organization; NAS:RGD.
DR   InterPro; IPR031794; HMMR_C.
DR   InterPro; IPR026203; IHABP.
DR   PANTHER; PTHR18956; PTHR18956; 1.
DR   Pfam; PF15908; HMMR_C; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Glycoprotein; Hyaluronic acid; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..498
FT                   /note="Hyaluronan-mediated motility receptor"
FT                   /id="PRO_0000084009"
FT   REGION          150..331
FT                   /note="Required for interaction with FAM83D"
FT                   /evidence="ECO:0000250|UniProtKB:O75330"
FT   REGION          420..430
FT                   /note="Hyaluronic acid-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          442..451
FT                   /note="Hyaluronic acid-binding"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         488
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O75330"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   498 AA;  57858 MW;  58037C79BD5C2A70 CRC64;
     MGGGVSYVGW LEKSETEKLL EYIEEISCAS DQVEKYKLDI AQLEEDLKEK DREILCLKQS
     LEEKVSFSKQ IEDLTVKCQL LEAERDDLVS KDRERAESLS AEMQVLTEKL LLERQEYEKL
     QQNELQSQSL LQQEKELSAH LQQQLCSFQE EMTSERNVFK EQLKLALDEL DAVQQKEEQS
     EKLVKQLEEE TKSTAEQLRR LDDLLREKEI ELEKRTAAHA QATVIAQEKY SDTAQTLRDV
     TAQLESYKSS TLKEIEDLKL ENLTLQEKVA MAEKRVEDVQ QQILTAESTN QEYAKVVQDL
     QNSSTLKEAE IKEITSSYLE KITDLQNQLR QQNEDFRKQL EEEGAKMTEK ETAVTELTME
     INKWRLLYEE LYDKTKPFQQ QLDAFEAEKQ ALLNEHGATQ EQLSKIRDSY AQLLGHQNLK
     QKIKHVVKLK DENSQLKSEV SKLRSQLAKR KQNELRLQGE LDKALGIRHF DPPKAFCHES
     KENVTLKTPL KEGNPNCC