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SRC kinase signaling inhibitor 1 (SNAP-25-interacting protein) (SNIP) (p130Cas-associated protein) (p140Cap)

 SRCN1_HUMAN             Reviewed;        1055 AA.
Q9C0H9; Q75T46; Q8N4W8;
16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
25-OCT-2017, entry version 139.
RecName: Full=SRC kinase signaling inhibitor 1;
AltName: Full=SNAP-25-interacting protein;
Short=SNIP;
AltName: Full=p130Cas-associated protein;
AltName: Full=p140Cap;
Name=SRCIN1; Synonyms=KIAA1684, P140;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:BAB21775.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Brain;
Sugiyama A., Inoue H., Oka M.;
"Homo sapiens cDNA, SNIP homolog.";
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Eye;
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).
[5] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 294-1055 (ISOFORM 1).
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:347-355(2000).
[6] {ECO:0000305}
PROTEIN SEQUENCE OF 306-325; 492-519; 583-593; 611-617; 700-719;
841-867; 884-895; 957-972; 983-1000 AND 1006-1017 (ISOFORM 1),
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BCAR1, AND
PHOSPHORYLATION.
PubMed=14657239; DOI=10.1091/mbc.E03-09-0689;
Di Stefano P., Cabodi S., Erba E.B., Margaria V., Bergatto E.,
Giuffrida M.G., Silengo L., Tarone G., Turco E., Defilippi P.;
"p130Cas-associated protein (p140Cap) as a new tyrosine-phosphorylated
protein involved in cell spreading.";
Mol. Biol. Cell 15:787-800(2004).
[7]
FUNCTION, AND INTERACTION WITH CSK AND SRC.
PubMed=17525734; DOI=10.1038/sj.emboj.7601724;
Di Stefano P., Damiano L., Cabodi S., Aramu S., Tordella L.,
Praduroux A., Piva R., Cavallo F., Forni G., Silengo L., Tarone G.,
Turco E., Defilippi P.;
"p140Cap protein suppresses tumour cell properties, regulating Csk and
Src kinase activity.";
EMBO J. 26:2843-2855(2007).
[8]
TISSUE SPECIFICITY.
PubMed=18475297; DOI=10.1038/sj.bjc.6604365;
Kennedy S., Clynes M., Doolan P., Mehta J.P., Rani S., Crown J.,
O'Driscoll L.;
"SNIP/p140Cap mRNA expression is an unfavourable prognostic factor in
breast cancer and is not expressed in normal breast tissue.";
Br. J. Cancer 98:1641-1645(2008).
[9]
INTERACTION WITH SORBS3 AND SYP.
PubMed=18662323; DOI=10.1111/j.1471-4159.2008.05585.x;
Ito H., Atsuzawa K., Sudo K., Di Stefano P., Iwamoto I., Morishita R.,
Takei S., Semba R., Defilippi P., Asano T., Usuda N., Nagata K.;
"Characterization of a multidomain adaptor protein, p140Cap, as part
of a pre-synaptic complex.";
J. Neurochem. 107:61-72(2008).
[10]
FUNCTION, INTERACTION WITH CTTN AND MAPRE3, AND SUBCELLULAR LOCATION.
PubMed=19146815; DOI=10.1016/j.neuron.2008.11.013;
Jaworski J., Kapitein L.C., Gouveia S.M., Dortland B.R., Wulf P.S.,
Grigoriev I., Camera P., Spangler S.A., Di Stefano P., Demmers J.,
Krugers H., Defilippi P., Akhmanova A., Hoogenraad C.C.;
"Dynamic microtubules regulate dendritic spine morphology and synaptic
plasticity.";
Neuron 61:85-100(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-729; SER-738
AND THR-756, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-52;
SER-53 AND SER-64 (ISOFORM 4), AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Acts as a negative regulator of SRC by activating CSK
which inhibits SRC activity and downstream signaling, leading to
impaired cell spreading and migration. Regulates dendritic spine
morphology. Involved in calcium-dependent exocytosis. May play a
role in neurotransmitter release or synapse maintenance.
{ECO:0000269|PubMed:14657239, ECO:0000269|PubMed:17525734,
ECO:0000269|PubMed:19146815}.
-!- SUBUNIT: Interacts with the N-terminal coiled-coil region of
SNAP25 (By similarity). Interacts with BCAR1/p130Cas and SRC
through its C-terminal domain. Interacts with CSK, CTTN,
SORBS3/vinexin, SYP and MAPRE3/EB3. {ECO:0000250,
ECO:0000269|PubMed:14657239, ECO:0000269|PubMed:17525734,
ECO:0000269|PubMed:18662323, ECO:0000269|PubMed:19146815}.
-!- INTERACTION:
P56945:BCAR1; NbExp=3; IntAct=EBI-1393949, EBI-702093;
P12931:SRC; NbExp=3; IntAct=EBI-1393949, EBI-621482;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell
projection, axon {ECO:0000250}. Cell projection, dendrite
{ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cell
junction, synapse, postsynaptic cell membrane, postsynaptic
density {ECO:0000250}. Note=Localized to the perinuclear region,
lamellopodia, cortical actin and actin stress fibers but not to
focal adhesions. Strongly expressed in axons and dendrites of the
CA1 and CA3 hippocampal regions and of the dentate gyrus. Detected
in both presynapses and postsynapses and in postsynaptic density
fractions.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1 {ECO:0000305};
IsoId=Q9C0H9-1; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=Q9C0H9-2; Sequence=VSP_050630;
Note=No experimental confirmation available. {ECO:0000305};
Name=3;
IsoId=Q9C0H9-4; Sequence=VSP_009366, VSP_009367, VSP_009368;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9C0H9-5; Sequence=VSP_039240;
Note=Ref.1 (BAD03968) sequence is in conflict in position:
177:L->P. Contains a phosphoserine at position 45. Contains a
phosphothreonine at position 52. Contains a phosphoserine at
position 53. Contains a phosphoserine at position 64.
{ECO:0000244|PubMed:24275569, ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in some primary breast carcinomas
where its presence is significantly associated with increased
tumor size. Not detected in normal breast tissue.
{ECO:0000269|PubMed:18475297}.
-!- PTM: Tyrosine-phosphorylated in response to EGF and to cell
adhesion to integrin ligands. {ECO:0000269|PubMed:14657239}.
-!- SIMILARITY: Belongs to the SRCIN1 family. {ECO:0000305}.
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EMBL; AB127405; BAD03968.1; -; mRNA.
EMBL; AK126665; BAC86634.1; -; mRNA.
EMBL; AC115090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC129916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC033233; AAH33233.1; -; mRNA.
EMBL; AB051471; BAB21775.1; -; mRNA.
CCDS; CCDS45660.1; -. [Q9C0H9-5]
RefSeq; NP_079524.2; NM_025248.2. [Q9C0H9-5]
UniGene; Hs.448872; -.
ProteinModelPortal; Q9C0H9; -.
SMR; Q9C0H9; -.
BioGrid; 123275; 11.
ELM; Q9C0H9; -.
IntAct; Q9C0H9; 4.
MINT; MINT-4777404; -.
STRING; 9606.ENSP00000264659; -.
ChEMBL; CHEMBL2150836; -.
iPTMnet; Q9C0H9; -.
PhosphoSitePlus; Q9C0H9; -.
BioMuta; SRCIN1; -.
DMDM; 296452948; -.
MaxQB; Q9C0H9; -.
PaxDb; Q9C0H9; -.
PeptideAtlas; Q9C0H9; -.
PRIDE; Q9C0H9; -.
DNASU; 80725; -.
Ensembl; ENST00000615049; ENSP00000480869; ENSG00000273608. [Q9C0H9-5]
Ensembl; ENST00000617146; ENSP00000484715; ENSG00000277363. [Q9C0H9-5]
GeneID; 80725; -.
KEGG; hsa:80725; -.
CTD; 80725; -.
DisGeNET; 80725; -.
EuPathDB; HostDB:ENSG00000277363.4; -.
GeneCards; SRCIN1; -.
H-InvDB; HIX0021064; -.
HGNC; HGNC:29506; SRCIN1.
HPA; HPA009701; -.
HPA; HPA063795; -.
MIM; 610786; gene.
neXtProt; NX_Q9C0H9; -.
OpenTargets; ENSG00000277363; -.
PharmGKB; PA165432823; -.
eggNOG; ENOG410IHFG; Eukaryota.
eggNOG; ENOG410XTBA; LUCA.
GeneTree; ENSGT00390000012399; -.
HOGENOM; HOG000293351; -.
HOVERGEN; HBG019587; -.
InParanoid; Q9C0H9; -.
KO; K19930; -.
OrthoDB; EOG091G00Q1; -.
PhylomeDB; Q9C0H9; -.
TreeFam; TF332255; -.
SIGNOR; Q9C0H9; -.
ChiTaRS; SRCIN1; human.
GenomeRNAi; 80725; -.
PRO; PR:Q9C0H9; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000277363; -.
ExpressionAtlas; Q9C0H9; baseline and differential.
GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0030175; C:filopodium; IEA:Ensembl.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
InterPro; IPR022782; AIP3_C.
InterPro; IPR026727; Srcin1.
PANTHER; PTHR22741:SF5; PTHR22741:SF5; 1.
Pfam; PF03915; AIP3; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Exocytosis; Membrane; Methylation;
Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
Synapse.
CHAIN 1 1055 SRC kinase signaling inhibitor 1.
/FTId=PRO_0000072011.
REGION 519 569 Interaction with SNAP25. {ECO:0000250}.
COILED 433 460 {ECO:0000255}.
COILED 521 546 {ECO:0000255}.
COILED 588 650 {ECO:0000255}.
COMPBIAS 343 376 Pro-rich.
COMPBIAS 828 886 Pro-rich.
MOD_RES 97 97 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 113 113 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 196 196 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 201 201 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 208 208 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 234 234 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 236 236 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 268 268 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 368 368 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 373 373 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 385 385 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 387 387 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 470 470 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 493 493 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 496 496 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 509 509 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 716 716 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 729 729 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 738 738 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 756 756 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 859 859 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 915 915 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 932 932 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
VAR_SEQ 1 566 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009366.
VAR_SEQ 1 52 MRGAWVHLHSGAASSLRPCRCGAGAAPKSSPRSPGGRRGDG
SSDSEGGVSFA -> MGNAPSQDPERSSPPMLSADDAEYPR
EYRTLGGGGGGGSGGRRFSNVGLVHTSERRHTVIAAQSLEA
LSGLQKADADRKRDAFMDHLKSKYPQHALALRGQQDRMREQ
PNYWSFKTRSSRHTQGAQPGLADQAAKLSYASAESLETMSE
AELPLGFSRMNRFRQSLPLSRSASQTKLRSP (in
isoform 4). {ECO:0000303|Ref.1}.
/FTId=VSP_039240.
VAR_SEQ 782 823 AAERDWEEKRAALTQYSAKDINRLLEETQAELLKAIPDLDC
A -> VLGPGIVGGAMSQVHTFLRPSFLEWGVPILWVFFLG
GGGPVP (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009367.
VAR_SEQ 824 1055 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009368.
VAR_SEQ 1012 1055 ATKPSKEMSGSNETSSPVSEKPSASRTSIPVLTSFGARNSS
ISF -> V (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_050630.
CONFLICT 314 314 Missing (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 481 481 T -> I (in Ref. 2; BAC86634).
{ECO:0000305}.
CONFLICT 592 592 L -> I (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 705 705 V -> M (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 713 714 LS -> IN (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 843 843 H -> E (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 850 850 R -> K (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 867 867 Y -> R (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 958 958 I -> L (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 987 987 Q -> P (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 994 994 S -> G (in Ref. 6; AA sequence).
{ECO:0000305}.
SEQUENCE 1055 AA; 112453 MW; CAB346DA20883EBD CRC64;
MRGAWVHLHS GAASSLRPCR CGAGAAPKSS PRSPGGRRGD GSSDSEGGVS FAGVLFLQFG
EETRRVHITH EVSSLDTLHA LIAHMFPQKL TMGMLKSPNT AILIKDEARN VFYELEDVRD
IQDRSIIKIY RKEPLYAAFP GSHLTNGDLR REMVYASRES SPTRRLNNLS PAPHLASGSP
PPGLPSGLPS GLQSGSPSRS RLSYAGGRPP SYAGSPVHHA AERLGGAPAA QGVSPSPSAI
LERRDVKPDE DLASKAGGMV LVKGEGLYAD PYGLLHEGRL SLAAAAGDPF AYPGAGGLYK
RGSVRSLSTY SAAALQSDLE DSLYKAAGGG GPLYGDGYGF RLPPSSPQKL ADVAAPPGGP
PPPHSPYSGP PSRGSPVRQS FRKDSGSSSV FAESPGGKTR SAGSASTAGA PPSELFPGPG
ERSLVGFGPP VPAKDTETRE RMEAMEKQIA SLTGLVQSAL LRGSEPETPS EKIEGSNGAA
TPSAPCGSGG RSSGATPVSG PPPPSASSTP AGQPTAVSRL QMQLHLRGLQ NSASDLRGQL
QQLRKLQLQN QESVRALLKR TEAELSMRVS EAARRQEDPL QRQRTLVEEE RLRYLNDEEL
ITQQLNDLEK SVEKIQRDVS HNHRLVPGPE LEEKALVLKQ LGETLTELKA HFPGLQSKMR
VVLRVEVEAV KFLKEEPQRL DGLLKRCRGV TDTLAQIRRQ VDEGVWPPPN NLLSQSPKKV
TAETDFNKSV DFEMPPPSPP LNLHELSGPA EGASLTPKGG NPTKGLDTPG KRSVDKAVSV
EAAERDWEEK RAALTQYSAK DINRLLEETQ AELLKAIPDL DCASKAHPGP APTPDHKPPK
APHGQKAAPR TEPSGRRGSD ELTVPRYRTE KPSKSPPPPP PRRSFPSSHG LTTTRTGEVV
VTSKKDSAFI KKAESEELEV QKPQVKLRRA VSEVARPAST PPIMASAIKD EDDEDRIIAE
LESGGGSVPP MKVVTPGASR LKAAQGQAGS PDKSKHGKQR AEYMRIQAQQ QATKPSKEMS
GSNETSSPVS EKPSASRTSI PVLTSFGARN SSISF


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