Primary Information |
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| BoMiProt ID | Bomi3717 |
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| Protein Name | Adhesion G protein-coupled receptor L1/Calcium-independent alpha-latrotoxin receptor 1/CIRL-1/Latrophilin-1 |
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| Organism | Bos taurus |
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| Uniprot ID | O97831 |
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| Milk Fraction | whey |
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| Ref Sequence ID | NP_001107200.1 |
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| Aminoacid Length | 1472 |
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| Molecular Weight | 162205 |
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| FASTA Sequence |
Download |
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| Gene Name | ADGRL1/LPHN1 |
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| Gene ID | 788252 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | It serves as calcium-independent receptor of high affinity for alpha-latrotoxin. |
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| Biochemical Properties | Interacts with syntaxin and with proteins of the SHANK family via the PDZ domain |
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| PTMs | Glycosylation, Methylation, Phosphorylation and Disulphide bond,Proteolytic cleavage |
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| Significance of PTMs | 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. |
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| Linking IDs | Bomi3717 |
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| Bibliography | Matsushita, H., Lelianova, V. G., & Ushkaryov, Y. A. (1999). The latrophilin family: multiply spliced G protein-coupled receptors with differential tissue distribution. FEBS letters, 443(3), 348–352. https://doi.org/10.1016/s0014-5793(99)00005-8 |
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| Protein Function | It serves as calcium-independent receptor of high affinity for alpha-latrotoxin. |
|---|
| Biochemical Properties | Interacts with syntaxin and with proteins of the SHANK family via the PDZ domain |
|---|
| PTMs | Glycosylation, Methylation, Phosphorylation and Disulphide bond,Proteolytic cleavage |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|O97831|AGRL1_BOVIN Adhesion G protein-coupled receptor L1 OS=Bos taurus OX=9913 GN=ADGRL1 PE=2 SV=1
MARLAAVLWSLCVTAILVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVEN
ANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNN*98RTQCVVVAGSDAFPDPCPGTYK
YLEVQYDCVPYKVKQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWI
PYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRT
RIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTL
RFEGTWETGYDKRSASNAFMVCGVLYVLRSVYVDDDSEAAGNRVDYAFNTNANREEPVSL
AFPNPYQFVSSVDYNPRDNQLYVWNNYFVVRYSLEFGPPDPSAGPATSPPLSTTTTARPT
PLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPAPSTRRPPAPNLHVSPELFC
EPREVRRVQWPATQQGMLVERPCPKGTRGIASFQCLPALGLWNPRGPDLSN*531CTSPWVNQV
AQKIKSGENAANIASELARHTRGSIYAGDVSSSVKLMEQLLDILDAQLQALRPIERESAG
KNYNKMHKRERTCKDYIKAVVETVDNLLRPEALESWKDMN*640ATEQAHTATMLLDVLEEGAF
LLADNVREPARFLAAKQNVVLEVTVLNTEGQVQELVFPQEYPSENSIQLSANTIKQNSRN
GVVKVVFILYNNLGLFLSTEN*741ATVKLAGEAGSGGPGGASLVVNSQVIAASINKESSRVFL
MDPVIFTVAHLEAKNHFNAN*800CSFWN*805YSERSMLGYWSTQGCRLVESN*826KTHTTCACSHLTNF
AVLMAHREIYQGRINELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCI
NLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYS
RTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVF
LMVTLHKMVRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYL
FTTFNAFQGVFIFVFHCALQKKVHKEYSKCLRHSYCCIRSPPGGAHGSLKTSAMRSNARY
YTGTQSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQPRGGTSPYN
TLIAESVGFNPSSPPVFNS*1219PGSYREPKHPLGGREACGMDTLPLNGNFNNSYSLRSGDFPP
GDGAPEPPRGRNLADAAAFEKMIISELVHNNLRGGSSGAKGPPPPEPPVPPVPGGSGEEE
AGGPGADRAEIELLYKALEEPLLLPRAQSVLYQSDLDESESCTAEDGATSRPLSSPPGRD
SLYASGANLRDSPSYPDSSPEGPSEALPPPPPAPPGPPEIYYTSRPPALVARNPLQGYYQ
VRRPSHEGYLAAPGLEGPGPDGDGQMQLVTS*1471L
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| Predicted Disorder Regions | 406-457, 1162-1263, 1295-1421 |
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| DisProt Annotation | |
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| TM Helix Prediction | 7TMHs; (7-25), (862-884), (928-950), (965-983), (1003-1025), (1048-1070), (1077-1095) |
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| Significance of PTMs | 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. |
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| Linking IDs | |
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| Bibliography | Matsushita, H., Lelianova, V. G., & Ushkaryov, Y. A. (1999). The latrophilin family: multiply spliced G protein-coupled receptors with differential tissue distribution. FEBS letters, 443(3), 348–352. https://doi.org/10.1016/s0014-5793(99)00005-8 |
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