ID   B1ALU1_HUMAN            Unreviewed;      1384 AA.
AC   B1ALU1;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   16-JAN-2019, entry version 108.
DE   SubName: Full=Adhesion G protein-coupled receptor L2 {ECO:0000313|Ensembl:ENSP00000359756};
GN   Name=ADGRL2 {ECO:0000313|Ensembl:ENSP00000359756};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000359756, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000359756, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S., Hart E., Haugen E., Heath P.D., Holmes S.,
RA   Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J.,
RA   James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K.,
RA   Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G.,
RA   Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J.,
RA   Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L.,
RA   Matthews N.S., McLaren S., Milne S., Mistry S., Moore M.J.,
RA   Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A.,
RA   Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K.,
RA   Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G.,
RA   Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N.,
RA   Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S.,
RA   Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L.,
RA   Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.,
RA   Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T.,
RA   Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R., Banerjee R.,
RA   Bryant S.P., Burford D.C., Burrill W.D., Clegg S.M., Dhami P.,
RA   Dovey O., Faulkner L.M., Gribble S.M., Langford C.F., Pandian R.D.,
RA   Porter K.M., Prigmore E.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [2] {ECO:0000213|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [3] {ECO:0000213|PubMed:21406692}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:rs3-RS3(2011).
RN   [4] {ECO:0000313|Ensembl:ENSP00000359756}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [5] {ECO:0000213|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       {ECO:0000256|SAAS:SAAS00547938}.
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DR   EMBL; AC093154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC095035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC113949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL138799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL157903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL358939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL359705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF510734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; B1ALU1; -.
DR   EPD; B1ALU1; -.
DR   jPOST; B1ALU1; -.
DR   MaxQB; B1ALU1; -.
DR   PeptideAtlas; B1ALU1; -.
DR   PRIDE; B1ALU1; -.
DR   Ensembl; ENST00000370721; ENSP00000359756; ENSG00000117114.
DR   UCSC; uc057hwx.1; human.
DR   EuPathDB; HostDB:ENSG00000117114.19; -.
DR   HGNC; HGNC:18582; ADGRL2.
DR   OpenTargets; ENSG00000117114; -.
DR   eggNOG; KOG3545; Eukaryota.
DR   eggNOG; KOG4193; Eukaryota.
DR   eggNOG; KOG4729; Eukaryota.
DR   eggNOG; ENOG410XSD2; LUCA.
DR   GeneTree; ENSGT00940000156348; -.
DR   HOGENOM; HOG000049065; -.
DR   HOVERGEN; HBG052337; -.
DR   ChiTaRS; ADGRL2; human.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000117114; Expressed in 103 organ(s), highest expression level in right lung.
DR   ExpressionAtlas; B1ALU1; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   Gene3D; 4.10.1240.10; -; 1.
DR   InterPro; IPR032471; GAIN_dom_N.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR003924; GPCR_2_latrophilin.
DR   InterPro; IPR003334; GPCR_2_latrophilin_rcpt_C.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   InterPro; IPR000203; GPS.
DR   InterPro; IPR031240; Latrophilin-2.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR003112; Olfac-like_dom.
DR   PANTHER; PTHR12011:SF61; PTHR12011:SF61; 2.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF16489; GAIN; 1.
DR   Pfam; PF02140; Gal_Lectin; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF02793; HRM; 1.
DR   Pfam; PF02354; Latrophilin; 1.
DR   Pfam; PF02191; OLF; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   PRINTS; PR01444; LATROPHILIN.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00008; HormR; 1.
DR   SMART; SM00284; OLF; 1.
DR   SUPFAM; SSF111418; SSF111418; 1.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS51132; OLF; 1.
DR   PROSITE; PS50228; SUEL_LECTIN; 1.
PE   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00446};
KW   G-protein coupled receptor {ECO:0000256|SAAS:SAAS00978998};
KW   Membrane {ECO:0000256|SAAS:SAAS00501090, ECO:0000256|SAM:Phobius};
KW   Proteomics identification {ECO:0000213|EPD:B1ALU1,
KW   ECO:0000213|MaxQB:B1ALU1, ECO:0000213|PeptideAtlas:B1ALU1};
KW   Receptor {ECO:0000256|SAAS:SAAS00978998};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transducer {ECO:0000256|SAAS:SAAS00978998};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00501090,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00501090,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26   1384       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002761805.
FT   TRANSMEM    770    795       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    807    825       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    831    855       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    876    896       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    916    939       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    960    983       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    989   1012       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       41    130       SUEL-type lectin.
FT                                {ECO:0000259|PROSITE:PS50228}.
FT   DOMAIN      139    398       Olfactomedin-like.
FT                                {ECO:0000259|PROSITE:PS51132}.
FT   DOMAIN      406    463       G_PROTEIN_RECEP_F2_3.
FT                                {ECO:0000259|PROSITE:PS50227}.
FT   DOMAIN      710    761       GPS. {ECO:0000259|PROSITE:PS50221}.
FT   DOMAIN      772   1013       G_PROTEIN_RECEP_F2_4.
FT                                {ECO:0000259|PROSITE:PS50261}.
FT   DISULFID    140    322       {ECO:0000256|PROSITE-ProRule:PRU00446}.
SQ   SEQUENCE   1384 AA;  155549 MW;  2B31FE00A57A2C58 CRC64;
     MVSSGCRMRS LWFIIVISFL PNTEGFSRAA LPFGLVRREL SCEGYSIDLR CPGSDVIMIE
     SANYGRTDDK ICDADPFQME NTDCYLPDAF KIMTQRCNNR TQCIVVTGSD VFPDPCPGTY
     KYLEVQYECV PYMEQKVFVC PGTLKAIVDS PCIYEAEQKA GAWCKDPLQA ADKIYFMPWT
     PYRTDTLIEY ASLEDFQNSR QTTTYKLPNR VDGTGFVVYD GAVFFNKERT RNIVKFDLRT
     RIKSGEAIIN YANYHDTSPY RWGGKTDIDL AVDENGLWVI YATEQNNGMI VISQLNPYTL
     RFEATWETVY DKRAASNAFM ICGVLYVVRS VYQDNESETG KNSIDYIYNT RLNRGEYVDV
     PFPNQYQYIA AVDYNPRDNQ LYVWNNNFIL RYSLEFGPPD PAQERFCEAL DSKGIKWPQT
     QRGMMVERPC PKGTRGTASY LCMISTGTWN PKGPDLSNCT SHWVNQLAQK IRSGENAASL
     ANELAKHTKG PVFAGDVSSS VRLMEQLVDI LDAQLQELKP SEKDSAGRSY NKAIVDTVDN
     LLRPEALESW KHMNSSEQAH TATMLLDTLE EGAFVLADNL LEPTRVSMPT ENIVLEVAVL
     STEGQIQDFK FPLGIKGAGS SIQLSANTVK QNSRNGLAKL VFIIYRSLGQ FLSTENATIK
     LGADFIGRNS TIAVNSHVIS VSINKESSRV YLTDPVLFTL PHIDPDNYFN ANCSFWNYSE
     RTMMGYWSTQ GCKLVDTNKT RTTCACSHLT NFAILMAHRE IAYKDGVHEL LLTVITWVGI
     VISLVCLAIC IFTFCFFRGL QSDRNTIHKN LCINLFIAEF IFLIGIDKTK YAIACPIFAG
     LLHFFFLAAF AWMCLEGVQL YLMLVEVFES EYSRKKYYYV AGYLFPATVV GVSAAIDYKS
     YGTEKACWLH VDNYFIWSFI GPVTFIILLN IIFLVITLCK MVKHSNTLKP DSSRLENIKS
     WVLGAFALLC LLGLTWSFGL LFINEETIVM AYLFTIFNAF QGVFIFIFHC ALQKKVRKEY
     GKCFRHSYCC GGLPTESPHS SVKASTTRTS ARYSSGTQSR IRRMWNDTVR KQSESSFISG
     DINSTSTLNQ GMTGNYLLTN PLLRPHGTNN PYNTLLAETV VCNAPSAPVF NSPGHSLNNA
     RDTSAMDTLP LNGNFNNSYS LHKGDYNDSV QVVDCGLSLN DTAFEKMIIS ELVHNNLRGS
     SKTHNLELTL PVKPVIGGSS SEDDAIVADA SSLMHSDNPG LELHHKELEA PLIPQRTHSL
     LYQPQKKVKS EGTDSYVSQL TAEAEDHLQS PNRDSLYTSM PNLRDSPYPE SSPDMEEDLS
     PSRRSENEDI YYKSMPNLGA GHQLQMCYQI SRGNSDGYII PINKEGCIPE GDVREGQMQL
     VTSL
//