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Protein

Hyaluronan-mediated motility receptor

Gene

Hmmr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in cell motility. When hyaluronan binds to HMMR, the phosphorylation of a number of proteins, including the PTK2/FAK1 occurs. May also be involved in cellular transformation and metastasis formation, and in regulating extracellular-regulated kinase (ERK) activity (By similarity).By similarity

GO - Molecular functioni

  • hyaluronic acid binding Source: RGD

GO - Biological processi

  • cell-cell signaling Source: RGD
  • cytoskeleton organization Source: RGD
Complete GO annotation...

Keywords - Ligandi

Hyaluronic acid

Names & Taxonomyi

Protein namesi
Recommended name:
Hyaluronan-mediated motility receptor
Alternative name(s):
Intracellular hyaluronic acid-binding protein
Receptor for hyaluronan-mediated motility
CD_antigen: CD168
Gene namesi
Name:Hmmr
Synonyms:Ihabp, Rhamm
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2805. Hmmr.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498Hyaluronan-mediated motility receptorPRO_0000084009Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence analysis
Glycosylationi302 – 3021N-linked (GlcNAc...)Sequence analysis
Glycosylationi483 – 4831N-linked (GlcNAc...)Sequence analysis
Modified residuei488 – 4881PhosphothreonineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiP97779.

Interactioni

Subunit structurei

Subunit of the HARC complex.

Protein-protein interaction databases

IntActiP97779. 1 interaction.
MINTiMINT-7138470.

Structurei

3D structure databases

ProteinModelPortaliP97779.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni420 – 43011Hyaluronic acid-bindingSequence analysisAdd
BLAST
Regioni442 – 45110Hyaluronic acid-bindingSequence analysis

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG044411.
InParanoidiP97779.

Family and domain databases

InterProiIPR031794. HMMR_C.
IPR031787. HMMR_N.
IPR026203. IHABP.
[Graphical view]
PANTHERiPTHR18956. PTHR18956. 1 hit.
PfamiPF15908. HMMR_C. 1 hit.
PF15905. HMMR_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97779-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGGVSYVGW LEKSETEKLL EYIEEISCAS DQVEKYKLDI AQLEEDLKEK
60 70 80 90 100
DREILCLKQS LEEKVSFSKQ IEDLTVKCQL LEAERDDLVS KDRERAESLS
110 120 130 140 150
AEMQVLTEKL LLERQEYEKL QQNELQSQSL LQQEKELSAH LQQQLCSFQE
160 170 180 190 200
EMTSERNVFK EQLKLALDEL DAVQQKEEQS EKLVKQLEEE TKSTAEQLRR
210 220 230 240 250
LDDLLREKEI ELEKRTAAHA QATVIAQEKY SDTAQTLRDV TAQLESYKSS
260 270 280 290 300
TLKEIEDLKL ENLTLQEKVA MAEKRVEDVQ QQILTAESTN QEYAKVVQDL
310 320 330 340 350
QNSSTLKEAE IKEITSSYLE KITDLQNQLR QQNEDFRKQL EEEGAKMTEK
360 370 380 390 400
ETAVTELTME INKWRLLYEE LYDKTKPFQQ QLDAFEAEKQ ALLNEHGATQ
410 420 430 440 450
EQLSKIRDSY AQLLGHQNLK QKIKHVVKLK DENSQLKSEV SKLRSQLAKR
460 470 480 490
KQNELRLQGE LDKALGIRHF DPPKAFCHES KENVTLKTPL KEGNPNCC
Length:498
Mass (Da):57,858
Last modified:May 1, 1997 - v1
Checksum:i58037C79BD5C2A70
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U87983 mRNA. Translation: AAB47997.1.
UniGeneiRn.92304.

Genome annotation databases

UCSCiRGD:2805. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U87983 mRNA. Translation: AAB47997.1.
UniGeneiRn.92304.

3D structure databases

ProteinModelPortaliP97779.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP97779. 1 interaction.
MINTiMINT-7138470.

Proteomic databases

PRIDEiP97779.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2805. rat.

Organism-specific databases

RGDi2805. Hmmr.

Phylogenomic databases

HOVERGENiHBG044411.
InParanoidiP97779.

Miscellaneous databases

PROiP97779.

Family and domain databases

InterProiIPR031794. HMMR_C.
IPR031787. HMMR_N.
IPR026203. IHABP.
[Graphical view]
PANTHERiPTHR18956. PTHR18956. 1 hit.
PfamiPF15908. HMMR_C. 1 hit.
PF15905. HMMR_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Savani R.C., Hou G.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Vascular smooth muscle.

Entry informationi

Entry nameiHMMR_RAT
AccessioniPrimary (citable) accession number: P97779
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: July 6, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.