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

 SRCN1_HUMAN             Reviewed;        1183 AA.
Q9C0H9; Q75T46; Q8N4W8;
16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 4.
05-DEC-2018, entry version 147.
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 1).
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 422-1183 (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 434-453; 620-647; 711-721; 739-745; 828-847;
969-995; 1012-1023; 1085-1100; 1111-1128 AND 1134-1145 (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-45; THR-52; SER-53;
SER-64; SER-364; SER-857; SER-866 AND THR-884, 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=3;
Name=1;
IsoId=Q9C0H9-5; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=Q9C0H9-2; Sequence=VSP_059451, VSP_059454;
Note=No experimental confirmation available. {ECO:0000305};
Name=3;
IsoId=Q9C0H9-4; Sequence=VSP_059450, VSP_059452, VSP_059453;
Note=No experimental confirmation available. {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; AC006449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC115090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC129916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC244153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KC877653; -; 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; 13.
ELM; Q9C0H9; -.
IntAct; Q9C0H9; 4.
MINT; Q9C0H9; -.
STRING; 9606.ENSP00000264659; -.
ChEMBL; CHEMBL2150836; -.
iPTMnet; Q9C0H9; -.
PhosphoSitePlus; Q9C0H9; -.
BioMuta; SRCIN1; -.
DMDM; 296452948; -.
EPD; Q9C0H9; -.
MaxQB; Q9C0H9; -.
PaxDb; Q9C0H9; -.
PeptideAtlas; Q9C0H9; -.
PRIDE; Q9C0H9; -.
ProteomicsDB; 80046; -.
ProteomicsDB; 80047; -. [Q9C0H9-2]
ProteomicsDB; 80048; -. [Q9C0H9-4]
ProteomicsDB; 80049; -. [Q9C0H9-5]
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; ENSGT00940000157961; -.
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; Expressed in 130 organ(s), highest expression level in C1 segment of cervical spinal cord.
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-like_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 1183 SRC kinase signaling inhibitor 1.
/FTId=PRO_0000072011.
REGION 647 697 Interaction with SNAP25.
{ECO:0000250|UniProtKB:Q9QXY2}.
COILED 654 674 {ECO:0000255}.
COILED 726 746 {ECO:0000255}.
COMPBIAS 471 504 Pro-rich.
COMPBIAS 956 1014 Pro-rich.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 52 52 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 53 53 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QXY2}.
MOD_RES 169 169 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QXY2}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 241 241 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 307 307 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 324 324 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 329 329 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 336 336 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 364 364 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 396 396 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 493 493 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 500 500 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 501 501 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 503 503 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 513 513 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 515 515 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 517 517 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 522 522 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 598 598 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 621 621 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 624 624 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 637 637 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 844 844 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 857 857 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 866 866 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 884 884 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 987 987 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 1043 1043 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
MOD_RES 1060 1060 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QWI6}.
VAR_SEQ 1 694 Missing (in isoform 3).
/FTId=VSP_059450.
VAR_SEQ 1 180 MGNAPSQDPERSSPPMLSADDAEYPREYRTLGGGGGGGSGG
RRFSNVGLVHTSERRHTVIAAQSLEALSGLQKADADRKRDA
FMDHLKSKYPQHALALRGQQDRMREQPNYWSFKTRSSRHTQ
GAQPGLADQAAKLSYASAESLETMSEAELPLGFSRMNRFRQ
SLPLSRSASQTKLRSP -> MRGAWVHLHSGAASSLRPCRC
GAGAAPKSSPRSPGGRRGDGSSDSEGGVSFA (in
isoform 2).
/FTId=VSP_059451.
VAR_SEQ 910 951 AAERDWEEKRAALTQYSAKDINRLLEETQAELLKAIPDLDC
A -> VLGPGIVGGAMSQVHTFLRPSFLEWGVPILWVFFLG
GGGPVP (in isoform 3).
/FTId=VSP_059452.
VAR_SEQ 952 1183 Missing (in isoform 3).
/FTId=VSP_059453.
VAR_SEQ 1141 1183 Missing (in isoform 2).
/FTId=VSP_059454.
CONFLICT 177 177 L -> P (in Ref. 1; BAD03968).
{ECO:0000305}.
CONFLICT 442 442 Missing (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 609 609 T -> I (in Ref. 2; BAC86634).
{ECO:0000305}.
CONFLICT 720 720 L -> I (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 833 833 V -> M (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 841 842 LS -> IN (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 971 971 H -> E (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 978 978 R -> K (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 995 995 Y -> R (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 1086 1086 I -> L (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 1115 1115 Q -> P (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 1122 1122 S -> G (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 1140 1140 A -> V (in Ref. 2; BAC86634).
{ECO:0000305}.
SEQUENCE 1183 AA; 127105 MW; 52BF566E715EF6FF CRC64;
MGNAPSQDPE RSSPPMLSAD DAEYPREYRT LGGGGGGGSG GRRFSNVGLV HTSERRHTVI
AAQSLEALSG LQKADADRKR DAFMDHLKSK YPQHALALRG QQDRMREQPN YWSFKTRSSR
HTQGAQPGLA DQAAKLSYAS AESLETMSEA ELPLGFSRMN RFRQSLPLSR SASQTKLRSP
GVLFLQFGEE TRRVHITHEV SSLDTLHALI AHMFPQKLTM GMLKSPNTAI LIKDEARNVF
YELEDVRDIQ DRSIIKIYRK EPLYAAFPGS HLTNGDLRRE MVYASRESSP TRRLNNLSPA
PHLASGSPPP GLPSGLPSGL QSGSPSRSRL SYAGGRPPSY AGSPVHHAAE RLGGAPAAQG
VSPSPSAILE RRDVKPDEDL ASKAGGMVLV KGEGLYADPY GLLHEGRLSL AAAAGDPFAY
PGAGGLYKRG SVRSLSTYSA AALQSDLEDS LYKAAGGGGP LYGDGYGFRL PPSSPQKLAD
VAAPPGGPPP PHSPYSGPPS RGSPVRQSFR KDSGSSSVFA ESPGGKTRSA GSASTAGAPP
SELFPGPGER SLVGFGPPVP AKDTETRERM EAMEKQIASL TGLVQSALLR GSEPETPSEK
IEGSNGAATP SAPCGSGGRS SGATPVSGPP PPSASSTPAG QPTAVSRLQM QLHLRGLQNS
ASDLRGQLQQ LRKLQLQNQE SVRALLKRTE AELSMRVSEA ARRQEDPLQR QRTLVEEERL
RYLNDEELIT QQLNDLEKSV EKIQRDVSHN HRLVPGPELE EKALVLKQLG ETLTELKAHF
PGLQSKMRVV LRVEVEAVKF LKEEPQRLDG LLKRCRGVTD TLAQIRRQVD EGVWPPPNNL
LSQSPKKVTA ETDFNKSVDF EMPPPSPPLN LHELSGPAEG ASLTPKGGNP TKGLDTPGKR
SVDKAVSVEA AERDWEEKRA ALTQYSAKDI NRLLEETQAE LLKAIPDLDC ASKAHPGPAP
TPDHKPPKAP HGQKAAPRTE PSGRRGSDEL TVPRYRTEKP SKSPPPPPPR RSFPSSHGLT
TTRTGEVVVT SKKDSAFIKK AESEELEVQK PQVKLRRAVS EVARPASTPP IMASAIKDED
DEDRIIAELE SGGGSVPPMK VVTPGASRLK AAQGQAGSPD KSKHGKQRAE YMRIQAQQQA
TKPSKEMSGS NETSSPVSEK PSASRTSIPV LTSFGARNSS ISF


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