Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-01431
Entry Name
UniProt Accession
Theoretical PI
6.21
Molecular Weight
166615.12
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Latrophilin-1
Protein Synonyms/Alias
Calcium-independent alpha-latrotoxin receptor 1; CIRL-1;
Gene Name
Lphn1
Gene Synonyms/Alias
Cirl; Cirl1; Cl1;
Created Date
26-APR-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
12
Canonical
AAALWSLCVTTVLVT
[1]
S-Palmitoylation
877
Canonical
SLVCLAICISTFCFL
[1]
S-Palmitoylation
882
Canonical
AICISTFCFLRGLQT
[1]
S-Palmitoylation
1117
Canonical
CLRHSYCCIRSPPGG
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Predicted from GPS-Lipid
Functional Description
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 propably implicated in the regulation of exocytosis.
Sequence Annotation
Topological domain: 25 857 Extracellular.
Transmembrane: 858 878 Helical; Name=1.
Topological domain: 879 892 Cytoplasmic.
Transmembrane: 893 913 Helical; Name=2.
Topological domain: 914 919 Extracellular.
Transmembrane: 920 940 Helical; Name=3.
Topological domain: 941 964 Cytoplasmic.
Transmembrane: 965 985 Helical; Name=4.
Topological domain: 986 1001 Extracellular.
Transmembrane: 1002 1022 Helical; Name=5.
Topological domain: 1023 1049 Cytoplasmic.
Transmembrane: 1050 1070 Helical; Name=6.
Topological domain: 1071 1074 Extracellular.
Transmembrane: 1075 1095 Helical; Name=7.
Topological domain: 1096 1515 Cytoplasmic.
Domain: 40 129 SUEL-type lectin.
Domain: 139 398 Olfactomedin-like.
Domain: 798 849 GPS.
Region: 117 120 Carbohydrate binding.
Binding site: 42 42 Carbohydrate.
Functional site: 837 838 Cleavage; by autocatalysis.
Protein Length
1515 AA.
Protein Sequence
(Canonical)
MARLAAALWS LCVTTVLVTS ATQGLSRAGL PFGLMRRELA CEGYPIELRC PGSDVIMVEN  60
ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT QCVVVAGSDA FPDPCPGTYK  120
YLEVQYDCVP YKVEQKVFVC PGTLQKVLEP TSTHESEHQS GAWCKDPLQA GDRIYVMPWI  180
PYRTDTLTEY ASWEDYVAAR HTTTYRLPNR VDGTGFVVYD GAVFYNKERT RNIVKYDLRT  240
RIKSGETVIN TANYHDTSPY RWGGKTDIDL AVDENGLWVI YATEGNNGRL VVSQLNPYTL  300
RFEGTWETGY DKRSASNAFM VCGVLYVLRS VYVDDDSEAA GNRVDYAFNT NANREEPVSL  360
AFPNPYQFVS SVDYNPRDNQ LYVWNNYFVV RYSLEFGPPD PSAGPATSPP LSTTTTARPT  420
PLTSTASPAA TTPLRRAPLT THPVGAINQL GPDLPPATAP APSTRRPPAP NLHVSPELFC  480
EPREVRRVQW PATQQGMLVE RPCPKGTRGI ASFQCLPALG LWNPRGPDLS NCTSPWVNQV  540
AQKIKSGENA ANIASELARH TRGSIYAGDV SSSVKLMEQL LDILDAQLQA LRPIERESAG  600
KNYNKMHKRE RTCKDYIKAV VETVDNLLRP EALESWKDMN ATEQVHTATM LLDVLEEGAF  660
LLADNVREPA RFLAAKQNVV LEVTVLSTEG QVQELVFPQE YASESSIQLS ANTIKQNSRN  720
GVVKVVFILY NNLGLFLSTE NATVKLAGEA GTGGPGGASL VVNSQVIAAS INKESSRVFL  780
MDPVIFTVAH LEAKNHFNAN CSFWNYSERS MLGYWSTQGC RLVESNKTHT TCACSHLTNF  840
AVLMAHREIY QGRINELLLS VITWVGIVIS LVCLAICIST FCFLRGLQTD RNTIHKNLCI  900
NLFLAELLFL VGIDKTQYEV ACPIFAGLLH YFFLAAFSWL CLEGVHLYLL LVEVFESEYS  960
RTKYYYLGGY CFPALVVGIA AAIDYRSYGT EKACWLRVDN YFIWSFIGPV SFVIVVNLVF  1020
LMVTLHKMIR SSSVLKPDSS RLDNIKSWAL GAIALLFLLG LTWAFGLLFI NKESVVMAYL  1080
FTTFNAFQGV FIFVFHCALQ KKVHKEYSKC LRHSYCCIRS PPGGAHGSLK TSAMRSNTRY  1140
YTGTQVPGQG RHIHQVSLGP RGRSALPESQ KDPGGQSGPG DPLTFGLCPS RIRRMWNDTV  1200
RKQTESSFMA GDINSTPTLN RGTMGNHLLT NPVLQPRGGT SPYNTLIAES VGFNPSSPPV  1260
FNSPGSYREP KHPLGGREAC GMDTLPLNGN FNNSYSLRSG DFPPGDGGPE PPRGRNLADA  1320
AAFEKMIISE LVHNNLRGAS GGAKGPPPEP PVPPVPGVSE DEAGGPGGAD RAEIELLYKA  1380
LEEPLLLPRA QSVLYQSDLD ESESCTAEDG ATSRPLSSPP GRDSLYASGA NLRDSPSYPD  1440
SSPEGPNEAL PPPPPAPPGP PEIYYTSRPP ALVARNPLQG YYQVRRPSHE GYLAAPSLEG  1500
PGPDGDGQMQ LVTSL                                                   1515
FASTA
(Canonical)
>LipidDB-10116-01431|O88917
MARLAAALWSLCVTTVLVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVEN
ANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYK
YLEVQYDCVPYKVEQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWI
PYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRT
RIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTL
RFEGTWETGYDKRSASNAFMVCGVLYVLRSVYVDDDSEAAGNRVDYAFNTNANREEPVSL
AFPNPYQFVSSVDYNPRDNQLYVWNNYFVVRYSLEFGPPDPSAGPATSPPLSTTTTARPT
PLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPAPSTRRPPAPNLHVSPELFC
EPREVRRVQWPATQQGMLVERPCPKGTRGIASFQCLPALGLWNPRGPDLSNCTSPWVNQV
AQKIKSGENAANIASELARHTRGSIYAGDVSSSVKLMEQLLDILDAQLQALRPIERESAG
KNYNKMHKRERTCKDYIKAVVETVDNLLRPEALESWKDMNATEQVHTATMLLDVLEEGAF
LLADNVREPARFLAAKQNVVLEVTVLSTEGQVQELVFPQEYASESSIQLSANTIKQNSRN
GVVKVVFILYNNLGLFLSTENATVKLAGEAGTGGPGGASLVVNSQVIAASINKESSRVFL
MDPVIFTVAHLEAKNHFNANCSFWNYSERSMLGYWSTQGCRLVESNKTHTTCACSHLTNF
AVLMAHREIYQGRINELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCI
NLFLAELLFLVGIDKTQYEVACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYS
RTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVF
LMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYL
FTTFNAFQGVFIFVFHCALQKKVHKEYSKCLRHSYCCIRSPPGGAHGSLKTSAMRSNTRY
YTGTQVPGQGRHIHQVSLGPRGRSALPESQKDPGGQSGPGDPLTFGLCPSRIRRMWNDTV
RKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQPRGGTSPYNTLIAESVGFNPSSPPV
FNSPGSYREPKHPLGGREACGMDTLPLNGNFNNSYSLRSGDFPPGDGGPEPPRGRNLADA
AAFEKMIISELVHNNLRGASGGAKGPPPEPPVPPVPGVSEDEAGGPGGADRAEIELLYKA
LEEPLLLPRAQSVLYQSDLDESESCTAEDGATSRPLSSPPGRDSLYASGANLRDSPSYPD
SSPEGPNEALPPPPPAPPGPPEIYYTSRPPALVARNPLQGYYQVRRPSHEGYLAAPSLEG
PGPDGDGQMQLVTSL
Gene Ontology
GO:0030424; C:axon; IDA:UniProtKB
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0030426; C:growth cone; IDA:UniProtKB
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0043005; C:neuron projection; IDA:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0014069; C:postsynaptic density; IDA:RGD
GO:0042734; C:presynaptic membrane; IDA:UniProtKB
GO:0045202; C:synapse; IDA:UniProtKB
GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW
GO:0050839; F:cell adhesion molecule binding; IDA:UniProtKB
GO:0004930; F:G-protein coupled receptor activity; IDA:RGD
GO:0016524; F:latrotoxin receptor activity; IDA:RGD
GO:0015643; F:toxic substance binding; IPI:RGD
GO:0007420; P:brain development; IEP:RGD
GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IDA:UniProtKB
GO:0007157; P:heterophilic cell-cell adhesion; IDA:UniProtKB
GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro
GO:0090129; P:positive regulation of synapse maturation; IDA:UniProtKB
GO:0016079; P:synaptic vesicle exocytosis; TAS:RGD
Interpro
InterPro; IPR022624; DUF3497
InterPro; IPR017981; GPCR_2-like
InterPro; IPR001879; GPCR_2_extracellular_dom
InterPro; IPR003924; GPCR_2_latrophilin
InterPro; IPR003334; GPCR_2_latrophilin_rcpt_C
InterPro; IPR000832; GPCR_2_secretin-like
InterPro; IPR017983; GPCR_2_secretin-like_CS
InterPro; IPR000203; GPS
InterPro; IPR000922; Lectin_gal-bd_dom
InterPro; IPR003112; Olfac-like
Pfam
Pfam; PF00002; 7tm_2;
Pfam; PF12003; DUF3497;
Pfam; PF02140; Gal_Lectin;
Pfam; PF01825; GPS;
Pfam; PF02793; HRM;
Pfam; PF02354; Latrophilin;
Pfam; PF02191; OLF;
SMART
SMART; SM00303; GPS;
SMART; SM00008; HormR;
SMART; SM00284; OLF;
PROSITE
PROSITE; PS00650; G_PROTEIN_RECEP_F2_2;
PROSITE; PS50227; G_PROTEIN_RECEP_F2_3;
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4;
PROSITE; PS50221; GPS;
PROSITE; PS51132; OLF;
PROSITE; PS50228; SUEL_LECTIN;
PRINTS
PRINTS; PR00249; GPCRSECRETIN;
PRINTS; PR01444; LATROPHILIN;