Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Adhesion G protein-coupled receptor L1

Gene

Adgrl1

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

Functioni

Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor probably implicated in the regulation of exocytosis.
Isoform 2: Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei42CarbohydrateBy similarity1

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB-KW
  • cell adhesion molecule binding Source: UniProtKB
  • G-protein coupled receptor activity Source: RGD
  • latrotoxin receptor activity Source: UniProtKB
  • toxic substance binding Source: RGD

GO - Biological processi

  • brain development Source: RGD
  • calcium-mediated signaling using intracellular calcium source Source: UniProtKB
  • cell surface receptor signaling pathway Source: InterPro
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  • positive regulation of synapse maturation Source: UniProtKB
  • synaptic vesicle exocytosis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Ligandi

Lectin

Protein family/group databases

MEROPSiP02.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Adhesion G protein-coupled receptor L1Imported
Alternative name(s):
Calcium-independent alpha-latrotoxin receptor 1Imported
Short name:
CIRL-11 Publication
Latrophilin-1Imported
Gene namesi
Name:Adgrl1Imported
Synonyms:Cirl1 Publication, Cirl1Imported, Cl11 Publication, Lphn1Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi620768. Adgrl1.

Subcellular locationi

Isoform 2 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 857ExtracellularSequence analysisAdd BLAST833
Transmembranei858 – 878Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini879 – 892CytoplasmicSequence analysisAdd BLAST14
Transmembranei893 – 913Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini914 – 919ExtracellularSequence analysis6
Transmembranei920 – 940Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini941 – 964CytoplasmicSequence analysisAdd BLAST24
Transmembranei965 – 985Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini986 – 1001ExtracellularSequence analysisAdd BLAST16
Transmembranei1002 – 1022Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini1023 – 1049CytoplasmicSequence analysisAdd BLAST27
Transmembranei1050 – 1070Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini1071 – 1074ExtracellularSequence analysis4
Transmembranei1075 – 1095Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini1096 – 1515CytoplasmicSequence analysisAdd BLAST420

GO - Cellular componenti

  • axon Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • growth cone Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • intracellular Source: GOC
  • neuron projection Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • postsynaptic density Source: RGD
  • presynaptic membrane Source: UniProtKB
  • synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi802S → R: Strongly reduced cleavage. 1 Publication1
Mutagenesisi804W → I: Abolishes cleavage. 1 Publication1
Mutagenesisi815W → S: Abolishes cleavage. Abolishes cell surface localization. 1 Publication1
Mutagenesisi834C → S: Strongly reduced cleavage. 2 Publications1
Mutagenesisi834C → W: Abolishes cleavage. Abolishes cell surface localization. 2 Publications1
Mutagenesisi836H → S: Abolishes cleavage. No effect on cell surface localization. 1 Publication1
Mutagenesisi837L → A: Abolishes cleavage. No effect on cell surface localization. 1 Publication1
Mutagenesisi838T → G: Abolishes cleavage. No effect on cell surface localization. 2 Publications1
Mutagenesisi838T → P: Abolishes cleavage. Abolishes cell surface localization. 2 Publications1
Mutagenesisi840F → A: Strongly reduced cleavage. 1 Publication1

Chemistry databases

GuidetoPHARMACOLOGYi206.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000001290825 – 1515Adhesion G protein-coupled receptor L1Add BLAST1491

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 71PROSITE-ProRule annotation
Disulfide bondi50 ↔ 128PROSITE-ProRule annotation
Disulfide bondi83 ↔ 115PROSITE-ProRule annotation
Disulfide bondi96 ↔ 102PROSITE-ProRule annotation
Glycosylationi98N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi140 ↔ 322PROSITE-ProRule annotation
Disulfide bondi480 ↔ 515PROSITE-ProRule annotation1 Publication
Disulfide bondi503 ↔ 532PROSITE-ProRule annotation1 Publication
Glycosylationi531N-linked (GlcNAc...)1 Publication1
Glycosylationi640N-linked (GlcNAc...)1 Publication1
Glycosylationi741N-linked (GlcNAc...)1 Publication1
Glycosylationi800N-linked (GlcNAc...)1 Publication1
Disulfide bondi801 ↔ 832PROSITE-ProRule annotation1 Publication
Glycosylationi805N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi820 ↔ 834PROSITE-ProRule annotation1 Publication
Glycosylationi826N-linked (GlcNAc...)1 Publication1
Modified residuei1237Omega-N-methylarginineBy similarity1
Modified residuei1263PhosphoserineBy similarity1
Modified residuei1497PhosphoserineBy similarity1
Modified residuei1514PhosphoserineBy similarity1

Post-translational modificationi

Autoproteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. This proteolytic processing takes place early in the biosynthetic pathway, either in the endoplasmic reticulum or in the early compartment of the Golgi apparatus.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei837 – 838Cleavage; by autolysis3 Publications2

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiO88917.
PRIDEiO88917.

PTM databases

iPTMnetiO88917.
PhosphoSitePlusiO88917.
SwissPalmiO88917.

Expressioni

Tissue specificityi

Expressed in the brain (at protein level). Brain specific distribution but low levels are also detected in most tissues.2 Publications

Gene expression databases

ExpressionAtlasiO88917. baseline and differential.

Interactioni

Subunit structurei

Forms a heterodimer, consisting of a large extracellular region (p120) non-covalently linked to a seven-transmembrane moiety (p85). Interacts with syntaxin and with proteins of the SHANK family via the PDZ domain (PubMed:9208860, PubMed:10958799). Isoform 2 interacts with TENM2 (PubMed:21724987). Interacts (via extracellular domain) with FLRT1, FLRT2 and FLRT3 (via extracellular domain) (By similarity).By similarity3 Publications

GO - Molecular functioni

  • cell adhesion molecule binding Source: UniProtKB

Protein-protein interaction databases

BioGridi249249. 2 interactors.
IntActiO88917. 1 interactor.
MINTiMINT-143437.
STRINGi10116.ENSRNOP00000042610.

Structurei

Secondary structure

11515
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi483 – 485Combined sources3
Beta strandi488 – 490Combined sources3
Beta strandi498 – 502Combined sources5
Beta strandi508 – 515Combined sources8
Turni517 – 519Combined sources3
Helixi536 – 545Combined sources10
Helixi550 – 560Combined sources11
Helixi567 – 590Combined sources24
Helixi605 – 627Combined sources23
Helixi630 – 632Combined sources3
Helixi633 – 636Combined sources4
Helixi641 – 663Combined sources23
Beta strandi668 – 675Combined sources8
Beta strandi677 – 687Combined sources11
Beta strandi695 – 697Combined sources3
Beta strandi704 – 709Combined sources6
Helixi711 – 716Combined sources6
Beta strandi722 – 732Combined sources11
Helixi733 – 736Combined sources4
Beta strandi759 – 762Combined sources4
Beta strandi766 – 773Combined sources8
Beta strandi779 – 789Combined sources11
Beta strandi796 – 806Combined sources11
Turni808 – 810Combined sources3
Beta strandi813 – 816Combined sources4
Beta strandi820 – 825Combined sources6
Beta strandi827 – 836Combined sources10
Beta strandi839 – 847Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DLQX-ray1.85A460-837[»]
B838-850[»]
ProteinModelPortaliO88917.
SMRiO88917.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 129SUEL-type lectinPROSITE-ProRule annotationAdd BLAST90
Domaini139 – 398Olfactomedin-likePROSITE-ProRule annotationAdd BLAST260
Domaini798 – 849GPSPROSITE-ProRule annotationAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni117 – 120Carbohydrate bindingBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi413 – 416Poly-Thr4
Compositional biasi1451 – 1461Poly-ProAdd BLAST11

Domaini

The extracellular domain coupled to the a single transmembrane region are sufficient for full responsiveness to alpha-latrotoxin.

Sequence similaritiesi

Contains 1 GPS domain.PROSITE-ProRule annotation
Contains 1 olfactomedin-like domain.PROSITE-ProRule annotation
Contains 1 SUEL-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3545. Eukaryota.
KOG4193. Eukaryota.
KOG4729. Eukaryota.
ENOG410XSD2. LUCA.
GeneTreeiENSGT00830000128227.
HOGENOMiHOG000049065.
HOVERGENiHBG052337.
InParanoidiO88917.
KOiK04592.
PhylomeDBiO88917.

Family and domain databases

InterProiIPR032471. GAIN_dom_N.
IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR003924. GPCR_2_latrophilin.
IPR003334. GPCR_2_latrophilin_rcpt_C.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR031234. Latrophilin-1.
IPR000922. Lectin_gal-bd_dom.
IPR003112. Olfac-like_dom.
[Graphical view]
PANTHERiPTHR12011:SF62. PTHR12011:SF62. 3 hits.
PfamiPF00002. 7tm_2. 1 hit.
PF16489. GAIN. 1 hit.
PF02140. Gal_Lectin. 1 hit.
PF01825. GPS. 1 hit.
PF02793. HRM. 1 hit.
PF02354. Latrophilin. 1 hit.
PF02191. OLF. 1 hit.
[Graphical view]
PRINTSiPR00249. GPCRSECRETIN.
PR01444. LATROPHILIN.
SMARTiSM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00284. OLF. 1 hit.
[Graphical view]
PROSITEiPS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
PS51132. OLF. 1 hit.
PS50228. SUEL_LECTIN. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O88917-1) [UniParc]FASTAAdd to basket
Also known as: CL1BB

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARLAAALWS LCVTTVLVTS ATQGLSRAGL PFGLMRRELA CEGYPIELRC
60 70 80 90 100
PGSDVIMVEN ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT
110 120 130 140 150
QCVVVAGSDA FPDPCPGTYK YLEVQYDCVP YKVEQKVFVC PGTLQKVLEP
160 170 180 190 200
TSTHESEHQS GAWCKDPLQA GDRIYVMPWI PYRTDTLTEY ASWEDYVAAR
210 220 230 240 250
HTTTYRLPNR VDGTGFVVYD GAVFYNKERT RNIVKYDLRT RIKSGETVIN
260 270 280 290 300
TANYHDTSPY RWGGKTDIDL AVDENGLWVI YATEGNNGRL VVSQLNPYTL
310 320 330 340 350
RFEGTWETGY DKRSASNAFM VCGVLYVLRS VYVDDDSEAA GNRVDYAFNT
360 370 380 390 400
NANREEPVSL AFPNPYQFVS SVDYNPRDNQ LYVWNNYFVV RYSLEFGPPD
410 420 430 440 450
PSAGPATSPP LSTTTTARPT PLTSTASPAA TTPLRRAPLT THPVGAINQL
460 470 480 490 500
GPDLPPATAP APSTRRPPAP NLHVSPELFC EPREVRRVQW PATQQGMLVE
510 520 530 540 550
RPCPKGTRGI ASFQCLPALG LWNPRGPDLS NCTSPWVNQV AQKIKSGENA
560 570 580 590 600
ANIASELARH TRGSIYAGDV SSSVKLMEQL LDILDAQLQA LRPIERESAG
610 620 630 640 650
KNYNKMHKRE RTCKDYIKAV VETVDNLLRP EALESWKDMN ATEQVHTATM
660 670 680 690 700
LLDVLEEGAF LLADNVREPA RFLAAKQNVV LEVTVLSTEG QVQELVFPQE
710 720 730 740 750
YASESSIQLS ANTIKQNSRN GVVKVVFILY NNLGLFLSTE NATVKLAGEA
760 770 780 790 800
GTGGPGGASL VVNSQVIAAS INKESSRVFL MDPVIFTVAH LEAKNHFNAN
810 820 830 840 850
CSFWNYSERS MLGYWSTQGC RLVESNKTHT TCACSHLTNF AVLMAHREIY
860 870 880 890 900
QGRINELLLS VITWVGIVIS LVCLAICIST FCFLRGLQTD RNTIHKNLCI
910 920 930 940 950
NLFLAELLFL VGIDKTQYEV ACPIFAGLLH YFFLAAFSWL CLEGVHLYLL
960 970 980 990 1000
LVEVFESEYS RTKYYYLGGY CFPALVVGIA AAIDYRSYGT EKACWLRVDN
1010 1020 1030 1040 1050
YFIWSFIGPV SFVIVVNLVF LMVTLHKMIR SSSVLKPDSS RLDNIKSWAL
1060 1070 1080 1090 1100
GAIALLFLLG LTWAFGLLFI NKESVVMAYL FTTFNAFQGV FIFVFHCALQ
1110 1120 1130 1140 1150
KKVHKEYSKC LRHSYCCIRS PPGGAHGSLK TSAMRSNTRY YTGTQVPGQG
1160 1170 1180 1190 1200
RHIHQVSLGP RGRSALPESQ KDPGGQSGPG DPLTFGLCPS RIRRMWNDTV
1210 1220 1230 1240 1250
RKQTESSFMA GDINSTPTLN RGTMGNHLLT NPVLQPRGGT SPYNTLIAES
1260 1270 1280 1290 1300
VGFNPSSPPV FNSPGSYREP KHPLGGREAC GMDTLPLNGN FNNSYSLRSG
1310 1320 1330 1340 1350
DFPPGDGGPE PPRGRNLADA AAFEKMIISE LVHNNLRGAS GGAKGPPPEP
1360 1370 1380 1390 1400
PVPPVPGVSE DEAGGPGGAD RAEIELLYKA LEEPLLLPRA QSVLYQSDLD
1410 1420 1430 1440 1450
ESESCTAEDG ATSRPLSSPP GRDSLYASGA NLRDSPSYPD SSPEGPNEAL
1460 1470 1480 1490 1500
PPPPPAPPGP PEIYYTSRPP ALVARNPLQG YYQVRRPSHE GYLAAPSLEG
1510
PGPDGDGQMQ LVTSL
Length:1,515
Mass (Da):166,615
Last modified:November 1, 1998 - v1
Checksum:i0BF3B900C54F17B7
GO
Isoform 2 (identifier: O88917-2) [UniParc]FASTAAdd to basket
Also known as: CL1AA

The sequence of this isoform differs from the canonical sequence as follows:
     132-137: KVEQKV → I
     1146-1189: Missing.

Show »
Length:1,466
Mass (Da):161,545
Checksum:i5926609E031565F9
GO
Isoform 3 (identifier: O88917-3) [UniParc]FASTAAdd to basket
Also known as: CL1AB

The sequence of this isoform differs from the canonical sequence as follows:
     132-137: KVEQKV → I

Show »
Length:1,510
Mass (Da):166,016
Checksum:i6A22505113DFCD5B
GO
Isoform 4 (identifier: O88917-4) [UniParc]FASTAAdd to basket
Also known as: CL1BA

The sequence of this isoform differs from the canonical sequence as follows:
     1146-1189: Missing.

Show »
Length:1,471
Mass (Da):162,144
Checksum:i9F560F544B4191C6
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_050398132 – 137KVEQKV → I in isoform 2 and isoform 3. 2 Publications6
Alternative sequenceiVSP_0503991146 – 1189Missing in isoform 2 and isoform 4. 3 PublicationsAdd BLAST44

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081144 mRNA. Translation: AAC62650.1.
AF081145 mRNA. Translation: AAC62651.1.
AF081146 mRNA. Translation: AAC62652.1.
AF081147 mRNA. Translation: AAC62653.1.
U72487 mRNA. Translation: AAC53268.1.
U78105 mRNA. Translation: AAC98700.1.
PIRiT17138.
T17145.
T17149.
T17156.
RefSeqiNP_075251.1. NM_022962.1. [O88917-4]
UniGeneiRn.10776.

Genome annotation databases

EnsembliENSRNOT00000045699; ENSRNOP00000043269; ENSRNOG00000029134. [O88917-4]
GeneIDi65096.
KEGGirno:65096.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081144 mRNA. Translation: AAC62650.1.
AF081145 mRNA. Translation: AAC62651.1.
AF081146 mRNA. Translation: AAC62652.1.
AF081147 mRNA. Translation: AAC62653.1.
U72487 mRNA. Translation: AAC53268.1.
U78105 mRNA. Translation: AAC98700.1.
PIRiT17138.
T17145.
T17149.
T17156.
RefSeqiNP_075251.1. NM_022962.1. [O88917-4]
UniGeneiRn.10776.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DLQX-ray1.85A460-837[»]
B838-850[»]
ProteinModelPortaliO88917.
SMRiO88917.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249249. 2 interactors.
IntActiO88917. 1 interactor.
MINTiMINT-143437.
STRINGi10116.ENSRNOP00000042610.

Chemistry databases

GuidetoPHARMACOLOGYi206.

Protein family/group databases

MEROPSiP02.010.
GPCRDBiSearch...

PTM databases

iPTMnetiO88917.
PhosphoSitePlusiO88917.
SwissPalmiO88917.

Proteomic databases

PaxDbiO88917.
PRIDEiO88917.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000045699; ENSRNOP00000043269; ENSRNOG00000029134. [O88917-4]
GeneIDi65096.
KEGGirno:65096.

Organism-specific databases

CTDi22859.
RGDi620768. Adgrl1.

Phylogenomic databases

eggNOGiKOG3545. Eukaryota.
KOG4193. Eukaryota.
KOG4729. Eukaryota.
ENOG410XSD2. LUCA.
GeneTreeiENSGT00830000128227.
HOGENOMiHOG000049065.
HOVERGENiHBG052337.
InParanoidiO88917.
KOiK04592.
PhylomeDBiO88917.

Miscellaneous databases

PROiO88917.

Gene expression databases

ExpressionAtlasiO88917. baseline and differential.

Family and domain databases

InterProiIPR032471. GAIN_dom_N.
IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR003924. GPCR_2_latrophilin.
IPR003334. GPCR_2_latrophilin_rcpt_C.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR031234. Latrophilin-1.
IPR000922. Lectin_gal-bd_dom.
IPR003112. Olfac-like_dom.
[Graphical view]
PANTHERiPTHR12011:SF62. PTHR12011:SF62. 3 hits.
PfamiPF00002. 7tm_2. 1 hit.
PF16489. GAIN. 1 hit.
PF02140. Gal_Lectin. 1 hit.
PF01825. GPS. 1 hit.
PF02793. HRM. 1 hit.
PF02354. Latrophilin. 1 hit.
PF02191. OLF. 1 hit.
[Graphical view]
PRINTSiPR00249. GPCRSECRETIN.
PR01444. LATROPHILIN.
SMARTiSM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00284. OLF. 1 hit.
[Graphical view]
PROSITEiPS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
PS51132. OLF. 1 hit.
PS50228. SUEL_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAGRL1_RAT
AccessioniPrimary (citable) accession number: O88917
Secondary accession number(s): O09026, O35818, O88916
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: November 1, 1998
Last modified: November 2, 2016
This is version 141 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.