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Adhesion G-protein coupled receptor G1 (G-protein coupled receptor 56) (Serpentine receptor cyt28) [Cleaved into: ADGRG1 N-terminal fragment (ADGRG1 NT) (GPR56 N-terminal fragment) (GPR56 NT) (GPR56(N)) (GPR56 extracellular subunit) (GPR56 subunit alpha); ADGRG1 C-terminal fragment (ADGRG1-CT) (GPR56 C-terminal fragment) (GPR56 CT) (GPR56(C)) (GPR56 seven-transmembrane subunit) (GPR56 7TM) (GPR56 subunit beta)]

 AGRG1_MOUSE             Reviewed;         687 AA.
Q8K209; Q3UR17; Q9QZT2;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-OCT-2017, entry version 132.
RecName: Full=Adhesion G-protein coupled receptor G1;
AltName: Full=G-protein coupled receptor 56;
AltName: Full=Serpentine receptor cyt28;
Contains:
RecName: Full=ADGRG1 N-terminal fragment;
Short=ADGRG1 NT;
AltName: Full=GPR56 N-terminal fragment;
Short=GPR56 NT;
Short=GPR56(N);
AltName: Full=GPR56 extracellular subunit;
AltName: Full=GPR56 subunit alpha;
Contains:
RecName: Full=ADGRG1 C-terminal fragment;
Short=ADGRG1-CT;
AltName: Full=GPR56 C-terminal fragment;
Short=GPR56 CT;
Short=GPR56(C);
AltName: Full=GPR56 seven-transmembrane subunit;
Short=GPR56 7TM;
AltName: Full=GPR56 subunit beta;
Flags: Precursor;
Name=Adgrg1 {ECO:0000312|MGI:MGI:1340051}; Synonyms=Cyt28, Gpr56;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Liver;
Phillips R.L., Ernst R.E., Dosil M., Wesley C.K., Moore K.A.,
Kingsley P.D., Sykes S., Palis J., Lemischka I.R.;
"Identification of novel hematopoietic stem cell regulatory genes.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Lung, Pituitary, Placenta, and Spinal ganglion;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-39; ASN-148;
ASN-171; ASN-234; ASN-303; ASN-324 AND ASN-341, AND MUTAGENESIS OF
ARG-38; TYR-88; CYS-91; CYS-346 AND TRP-349.
PubMed=17576745; DOI=10.1093/hmg/ddm144;
Jin Z., Tietjen I., Bu L., Liu-Yesucevitz L., Gaur S.K., Walsh C.A.,
Piao X.;
"Disease-associated mutations affect GPR56 protein trafficking and
cell surface expression.";
Hum. Mol. Genet. 16:1972-1985(2007).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18509043; DOI=10.1523/JNEUROSCI.0853-08.2008;
Li S., Jin Z., Koirala S., Bu L., Xu L., Hynes R.O., Walsh C.A.,
Corfas G., Piao X.;
"GPR56 regulates pial basement membrane integrity and cortical
lamination.";
J. Neurosci. 28:5817-5826(2008).
[6]
FUNCTION.
PubMed=18378689; DOI=10.1074/jbc.M708919200;
Iguchi T., Sakata K., Yoshizaki K., Tago K., Mizuno N., Itoh H.;
"Orphan G protein-coupled receptor GPR56 regulates neural progenitor
cell migration via a G alpha 12/13 and Rho pathway.";
J. Biol. Chem. 283:14469-14478(2008).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19515912; DOI=10.1523/JNEUROSCI.1182-09.2009;
Koirala S., Jin Z., Piao X., Corfas G.;
"GPR56-regulated granule cell adhesion is essential for rostral
cerebellar development.";
J. Neurosci. 29:7439-7449(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=20981830; DOI=10.1002/dvdy.22468;
Chen G., Yang L., Begum S., Xu L.;
"GPR56 is essential for testis development and male fertility in
mice.";
Dev. Dyn. 239:3358-3367(2010).
[10]
FUNCTION, TISSUE SPECIFICITY, AND LIGAND-BINDING.
PubMed=21768377; DOI=10.1073/pnas.1104821108;
Luo R., Jeong S.J., Jin Z., Strokes N., Li S., Piao X.;
"G protein-coupled receptor 56 and collagen III, a receptor-ligand
pair, regulates cortical development and lamination.";
Proc. Natl. Acad. Sci. U.S.A. 108:12925-12930(2011).
[11]
LIGAND-BINDING, AND MUTAGENESIS OF ARG-38; TYR-88 AND CYS-91.
PubMed=22238662; DOI=10.1371/journal.pone.0029818;
Luo R., Jin Z., Deng Y., Strokes N., Piao X.;
"Disease-associated mutations prevent GPR56-collagen III
interaction.";
PLoS ONE 7:E29818-E29818(2012).
[12]
FUNCTION.
PubMed=23478665; DOI=10.1038/leu.2013.75;
Saito Y., Kaneda K., Suekane A., Ichihara E., Nakahata S.,
Yamakawa N., Nagai K., Mizuno N., Kogawa K., Miura I., Itoh H.,
Morishita K.;
"Maintenance of the hematopoietic stem cell pool in bone marrow niches
by EVI1-regulated GPR56.";
Leukemia 27:1637-1649(2013).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24531968; DOI=10.1126/science.1244392;
Bae B.I., Tietjen I., Atabay K.D., Evrony G.D., Johnson M.B.,
Asare E., Wang P.P., Murayama A.Y., Im K., Lisgo S.N., Overman L.,
Sestan N., Chang B.S., Barkovich A.J., Grant P.E., Topcu M.,
Politsky J., Okano H., Piao X., Walsh C.A.;
"Evolutionarily dynamic alternative splicing of GPR56 regulates
regional cerebral cortical patterning.";
Science 343:764-768(2014).
[14]
INTERACTION WITH HEPARIN.
PubMed=27068534; DOI=10.1242/jcs.174458;
Chiang N.Y., Chang G.W., Huang Y.S., Peng Y.M., Hsiao C.C., Kuo M.L.,
Lin H.H.;
"Heparin interacts with adhesion-GPCR GPR56/ADGRG1, reduces receptor
shedding, and promotes cell adhesion and motility.";
J. Cell Sci. 129:2156-2169(2016).
-!- FUNCTION: Receptor involved in cell adhesion and probably in cell-
cell interactions. Mediates cell matrix adhesion in developing
neurons and hematopoietic stem cells. Receptor for collagen
III/COL3A1 in the developing brain and involved in regulation of
cortical development, specifically in maintenance of the pial
basement membrane integrity and in cortical lamination
(PubMed:21768377). Binding to the COL3A1 ligand inhibits neuronal
migration and activates the RhoA pathway by coupling to GNA13 and
possibly GNA12 (By similarity). Plays a role in the maintenance of
hematopoietic stem cells and/or leukemia stem cells in bone marrow
niche (PubMed:23478665). Plays a critical role in tumourigenesis
(By similarity). Plays essential role in testis development
(PubMed:20981830). {ECO:0000250|UniProtKB:Q9Y653,
ECO:0000269|PubMed:18378689, ECO:0000269|PubMed:18509043,
ECO:0000269|PubMed:19515912, ECO:0000269|PubMed:20981830,
ECO:0000269|PubMed:21768377, ECO:0000269|PubMed:23478665,
ECO:0000269|PubMed:24531968}.
-!- ENZYME REGULATION: ADGRG1 NT is proposed to inhibit receptor
signaling; its interactions with extracellular ligands and /or
homophilic ADGRG1 NT interactions may relieve the inhibition.
Following ligand binding to the N-terminal fragment, the N-
terminal fragment is released from the seven-transmembrane C-
terminal fragment to unveil a new N-terminal stalk, which then
stimulates G-protein-dependent signaling activity. The N-terminal
stalk has also been shown to be dispensable for at least some G-
protein-dependent signaling. {ECO:0000250|UniProtKB:Q9Y653}.
-!- SUBUNIT: Predominantly non-covalently linked heterodimer of the N-
terminal and the C-terminal fragment. ADGRG1 NT self-associates in
a trans-trans manner; the homophilic interaction enhances receptor
signaling. ADGRG1 CT interacts with ARRB2; the interaction is
impaired by ADGRG1 NT. Part of a GPCR-tetraspanin complex at least
consisting of ADGRG1, CD81, eventually CD9, and GNA11 in which
CD81 is enhancing the association of ADGRG1 with GNA11 (By
similarity). Interacts with heparin; leading to the reduction of
ADGRG1 shedding (PubMed:27068534). {ECO:0000250|UniProtKB:Q9Y653,
ECO:0000269|PubMed:27068534}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17576745,
ECO:0000269|PubMed:22238662}; Multi-pass membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: ADGRG1 N-terminal fragment: Secreted
{ECO:0000250|UniProtKB:Q9Y653}.
-!- SUBCELLULAR LOCATION: ADGRG1 C-terminal fragment: Membrane raft
{ECO:0000250|UniProtKB:Q9Y653}. Note=Interaction with its ligand
COL3A1 leads to the release of ADGRG1 NT from the membrane and
triggers the association of ADGRG1 CT with lipid rafts.
{ECO:0000250|UniProtKB:Q9Y653}.
-!- TISSUE SPECIFICITY: Expressed in neural progenitor cells in fetal
forbrain. Expressed in migrating neurons. Expressed in radial
glial endfeet (at protein level) (PubMed:21768377). Expressed in
peritubular myoid cells, Sertoli cells, and germ cells of the
testis (PubMed:20981830). {ECO:0000269|PubMed:20981830,
ECO:0000269|PubMed:21768377}.
-!- PTM: Autoproteolytically cleaved into 2 fragments; the large
extracellular N-terminal fragment and the membroune-bound C-
terminal fragment predominantly remain associated and non-
covalently linked. {ECO:0000269|PubMed:22238662}.
-!- PTM: N-glycosylated. The secreted ADGRG1 N-terminal fragment is
heavily glycosylated. {ECO:0000269|PubMed:17576745}.
-!- PTM: Ubiquitinated. Undergoes polyubiquitination upon activation.
{ECO:0000250|UniProtKB:Q9Y653}.
-!- DISRUPTION PHENOTYPE: Cobblestone-like cortical malformation with
defective pial basement membrane (BM), abnormal anchorage of
radial glial endfeet, mislocalized Cajal-Retzius cells and
neuronal overmigration. Severe malformation of the rostral
cerebellum that develops perinatally. Granule cells from the
rostral region show loss of adhesion to extracellular matrix
molecules of the pial basement membrane. In ADGRG1 knockout mice,
neurons overmigrate through breached pial basement membrane or
undermigrate forming irregular cortical layers. Deficient mice
shown disruption of seminiferous tubule formation and increased
sterility (PubMed:20981830). {ECO:0000269|PubMed:18509043,
ECO:0000269|PubMed:20981830, ECO:0000269|PubMed:24531968}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
LN-TM7 subfamily. {ECO:0000305}.
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EMBL; AF166382; AAF00617.1; -; mRNA.
EMBL; AK087268; BAC39835.1; -; mRNA.
EMBL; AK133678; BAE21780.1; -; mRNA.
EMBL; AK141886; BAE24871.1; -; mRNA.
EMBL; AK141894; BAE24874.1; -; mRNA.
EMBL; AK167547; BAE39613.1; -; mRNA.
EMBL; BC034678; AAH34678.1; -; mRNA.
CCDS; CCDS22553.1; -.
RefSeq; NP_001185823.1; NM_001198894.1.
RefSeq; NP_061370.2; NM_018882.3.
RefSeq; XP_006530755.1; XM_006530692.2.
RefSeq; XP_006530756.1; XM_006530693.2.
RefSeq; XP_006530757.1; XM_006530694.2.
RefSeq; XP_006530758.1; XM_006530695.2.
RefSeq; XP_006530759.1; XM_006530696.3.
RefSeq; XP_006530760.1; XM_006530697.2.
UniGene; Mm.290834; -.
PDB; 5KVM; X-ray; 2.45 A; A=28-382, B=383-391.
PDBsum; 5KVM; -.
ProteinModelPortal; Q8K209; -.
SMR; Q8K209; -.
IntAct; Q8K209; 1.
STRING; 10090.ENSMUSP00000090959; -.
MEROPS; P02.008; -.
iPTMnet; Q8K209; -.
PhosphoSitePlus; Q8K209; -.
MaxQB; Q8K209; -.
PaxDb; Q8K209; -.
PeptideAtlas; Q8K209; -.
PRIDE; Q8K209; -.
Ensembl; ENSMUST00000093271; ENSMUSP00000090959; ENSMUSG00000031785.
Ensembl; ENSMUST00000179619; ENSMUSP00000137520; ENSMUSG00000031785.
Ensembl; ENSMUST00000212660; ENSMUSP00000148644; ENSMUSG00000031785.
GeneID; 14766; -.
KEGG; mmu:14766; -.
UCSC; uc009mxl.2; mouse.
CTD; 9289; -.
MGI; MGI:1340051; Adgrg1.
eggNOG; KOG4193; Eukaryota.
eggNOG; ENOG410XSD2; LUCA.
GeneTree; ENSGT00900000140853; -.
HOGENOM; HOG000015136; -.
HOVERGEN; HBG051814; -.
InParanoid; Q8K209; -.
KO; K08450; -.
OMA; SMCWIRD; -.
OrthoDB; EOG091G02U6; -.
PhylomeDB; Q8K209; -.
TreeFam; TF321769; -.
ChiTaRS; Gpr56; mouse.
PRO; PR:Q8K209; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031785; -.
CleanEx; MM_GPR56; -.
ExpressionAtlas; Q8K209; baseline and differential.
Genevisible; Q8K209; MM.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0097451; C:glial limiting end-foot; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
GO; GO:0050840; F:extracellular matrix binding; IDA:UniProtKB.
GO; GO:0004930; F:G-protein coupled receptor activity; IMP:UniProtKB.
GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
GO; GO:0007420; P:brain development; ISO:MGI.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0021801; P:cerebral cortex radial glia guided migration; IMP:UniProtKB.
GO; GO:0021796; P:cerebral cortex regionalization; IMP:MGI.
GO; GO:0021819; P:layer formation in cerebral cortex; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:2001223; P:negative regulation of neuron migration; IMP:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:MGI.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:UniProtKB.
GO; GO:0070528; P:protein kinase C signaling; ISS:UniProtKB.
GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB.
GO; GO:0072520; P:seminiferous tubule development; IMP:UniProtKB.
GO; GO:0010573; P:vascular endothelial growth factor production; ISS:UniProtKB.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR003910; GPR1/GPR3/GPR5.
InterPro; IPR000203; GPS.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF01825; GPS; 1.
PRINTS; PR00249; GPCRSECRETIN.
PRINTS; PR01422; GPR56ORPHANR.
SMART; SM00303; GPS; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PROSITE; PS50221; GPS; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell membrane; Complete proteome;
Developmental protein; Differentiation; G-protein coupled receptor;
Glycoprotein; Heparin-binding; Membrane; Neurogenesis; Receptor;
Reference proteome; Secreted; Signal; Transducer; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 25 {ECO:0000250|UniProtKB:Q9Y653}.
CHAIN 26 687 Adhesion G-protein coupled receptor G1.
/FTId=PRO_0000012882.
CHAIN 26 ?382 ADGRG1 N-terminal fragment.
{ECO:0000250|UniProtKB:Q9Y653}.
/FTId=PRO_0000436505.
CHAIN ?383 687 ADGRG1 C-terminal fragment.
{ECO:0000250|UniProtKB:Q9Y653}.
/FTId=PRO_0000436506.
TOPO_DOM 26 402 Extracellular. {ECO:0000255}.
TRANSMEM 403 423 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 424 442 Cytoplasmic. {ECO:0000255}.
TRANSMEM 443 463 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 464 471 Extracellular. {ECO:0000255}.
TRANSMEM 472 492 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 493 512 Cytoplasmic. {ECO:0000255}.
TRANSMEM 513 533 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 534 570 Extracellular. {ECO:0000255}.
TRANSMEM 571 591 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 592 603 Cytoplasmic. {ECO:0000255}.
TRANSMEM 604 624 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 625 630 Extracellular. {ECO:0000255}.
TRANSMEM 631 651 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 652 687 Cytoplasmic. {ECO:0000255}.
DOMAIN 343 394 GPS. {ECO:0000255|PROSITE-
ProRule:PRU00098}.
REGION 26 33 Heparin-binding.
{ECO:0000250|UniProtKB:Q9Y653}.
REGION 190 200 Heparin-binding.
{ECO:0000250|UniProtKB:Q9Y653}.
SITE 382 383 Cleavage; by autolysis.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17576745}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17576745}.
CARBOHYD 171 171 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17576745}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17576745}.
CARBOHYD 303 303 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17576745}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17576745}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17576745}.
MUTAGEN 38 38 R->Q,W: Reduced cell surface
localization.
{ECO:0000269|PubMed:17576745,
ECO:0000269|PubMed:22238662}.
MUTAGEN 88 88 Y->C: Reduced cell surface localization.
{ECO:0000269|PubMed:17576745,
ECO:0000269|PubMed:22238662}.
MUTAGEN 91 91 C->S: Reduced cell surface localization.
{ECO:0000269|PubMed:17576745,
ECO:0000269|PubMed:22238662}.
MUTAGEN 346 346 C->S: Abolishes proteolytic cleavage and
cell surface localization.
{ECO:0000269|PubMed:17576745}.
MUTAGEN 349 349 W->S: Abolishes proteolytic cleavage and
cell surface localization.
{ECO:0000269|PubMed:17576745}.
CONFLICT 643 643 F -> Y (in Ref. 1; AAF00617).
{ECO:0000305}.
STRAND 31 40 {ECO:0000244|PDB:5KVM}.
STRAND 45 50 {ECO:0000244|PDB:5KVM}.
STRAND 52 54 {ECO:0000244|PDB:5KVM}.
STRAND 56 60 {ECO:0000244|PDB:5KVM}.
STRAND 62 71 {ECO:0000244|PDB:5KVM}.
STRAND 86 95 {ECO:0000244|PDB:5KVM}.
TURN 96 99 {ECO:0000244|PDB:5KVM}.
STRAND 100 105 {ECO:0000244|PDB:5KVM}.
STRAND 108 114 {ECO:0000244|PDB:5KVM}.
STRAND 124 126 {ECO:0000244|PDB:5KVM}.
STRAND 136 145 {ECO:0000244|PDB:5KVM}.
STRAND 155 160 {ECO:0000244|PDB:5KVM}.
HELIX 176 191 {ECO:0000244|PDB:5KVM}.
HELIX 193 195 {ECO:0000244|PDB:5KVM}.
STRAND 196 198 {ECO:0000244|PDB:5KVM}.
HELIX 202 218 {ECO:0000244|PDB:5KVM}.
STRAND 222 230 {ECO:0000244|PDB:5KVM}.
STRAND 233 239 {ECO:0000244|PDB:5KVM}.
HELIX 242 246 {ECO:0000244|PDB:5KVM}.
STRAND 249 252 {ECO:0000244|PDB:5KVM}.
STRAND 259 269 {ECO:0000244|PDB:5KVM}.
HELIX 271 274 {ECO:0000244|PDB:5KVM}.
STRAND 287 294 {ECO:0000244|PDB:5KVM}.
HELIX 308 310 {ECO:0000244|PDB:5KVM}.
STRAND 311 317 {ECO:0000244|PDB:5KVM}.
STRAND 329 335 {ECO:0000244|PDB:5KVM}.
STRAND 343 350 {ECO:0000244|PDB:5KVM}.
TURN 353 355 {ECO:0000244|PDB:5KVM}.
STRAND 360 362 {ECO:0000244|PDB:5KVM}.
STRAND 366 370 {ECO:0000244|PDB:5KVM}.
STRAND 372 381 {ECO:0000244|PDB:5KVM}.
STRAND 384 390 {ECO:0000244|PDB:5KVM}.
SEQUENCE 687 AA; 77255 MW; B5315D70B66C9A9A CRC64;
MAVQVLRQMV YFLLSLFSLV QGAHSGSPRE DFRFCGQRNQ TQQSTLHYDQ SSEPHIFVWN
TEETLTIRAP FLAAPDIPRF FPEPRGLYHF CLYWSRHTGR LHLRYGKHDY LLSSQASRLL
CFQKQEQSLK QGAPLIATSV SSWQIPQNTS LPGAPSFIFS FHNAPHKVSH NASVDMCDLK
KELQQLSRYL QHPQKAAKRP TAAFISQQLQ SLESKLTSVS FLGDTLSFEE DRVNATVWKL
PPTAGLEDLH IHSQKEEEQS EVQAYSLLLP RAVFQQTRGR RRDDAKRLLV VDFSSQALFQ
DKNSSQVLGE KVLGIVVQNT KVTNLSDPVV LTFQHQPQPK NVTLQCVFWV EDPASSSTGS
WSSAGCETVS RDTQTSCLCN HLTYFAVLMV SSTEVEATHK HYLTLLSYVG CVISALACVF
TIAAYLCSRR KSRDYTIKVH MNLLSAVFLL DVSFLLSEPV ALTGSEAACR TSAMFLHFSL
LACLSWMGLE GYNLYRLVVE VFGTYVPGYL LKLSIVGWGF PVFLVTLVAL VDVNNYGPII
LAVRRTPERV TYPSMCWIRD SLVSYVTNLG LFSLVFLFNL AMLATMVVQI LRLRPHSQNW
PHVLTLLGLS LVLGLPWALV FFSFASGTFQ LVILYLFSII TSFQGFLIFL WYWSMRFQAQ
GGPSPLKNNS DSAKLPISSG STSSSRI


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