SRCN1_RAT
ID SRCN1_RAT Reviewed; 1197 AA.
AC Q9QXY2; Q9QXY3;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=SRC kinase signaling inhibitor 1 {ECO:0000305};
DE AltName: Full=SNAP-25-interacting protein;
DE Short=SNIP;
DE AltName: Full=p130Cas-associated protein;
DE AltName: Full=p140Cap {ECO:0000303|PubMed:18662323};
GN Name=Srcin1 {ECO:0000312|RGD:708439};
GN Synonyms=P140 {ECO:0000303|PubMed:18662323},
GN Snip {ECO:0000303|PubMed:22673903};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAF25004.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH SNAP25.
RX PubMed=10625663; DOI=10.1074/jbc.275.2.1191;
RA Chin L.-S., Nugent R.D., Raynor M.C., Vavalle J.P., Li L.;
RT "SNIP, a novel SNAP-25-interacting protein implicated in regulated
RT exocytosis.";
RL J. Biol. Chem. 275:1191-1200(2000).
RN [2]
RP INTERACTION WITH SORBS3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=18662323; DOI=10.1111/j.1471-4159.2008.05585.x;
RA Ito H., Atsuzawa K., Sudo K., Di Stefano P., Iwamoto I., Morishita R.,
RA Takei S., Semba R., Defilippi P., Asano T., Usuda N., Nagata K.;
RT "Characterization of a multidomain adaptor protein, p140Cap, as part of a
RT pre-synaptic complex.";
RL J. Neurochem. 107:61-72(2008).
RN [3]
RP FUNCTION, INTERACTION WITH MAPRE3, AND SUBCELLULAR LOCATION.
RX PubMed=19146815; DOI=10.1016/j.neuron.2008.11.013;
RA Jaworski J., Kapitein L.C., Gouveia S.M., Dortland B.R., Wulf P.S.,
RA Grigoriev I., Camera P., Spangler S.A., Di Stefano P., Demmers J.,
RA Krugers H., Defilippi P., Akhmanova A., Hoogenraad C.C.;
RT "Dynamic microtubules regulate dendritic spine morphology and synaptic
RT plasticity.";
RL Neuron 61:85-100(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-178; SER-200;
RP SER-204; SER-260; SER-378; SER-547; SER-556; SER-900; SER-1021 AND
RP SER-1077, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Acts as a negative regulator of SRC by activating CSK which
CC inhibits SRC activity and downstream signaling, leading to impaired
CC cell spreading and migration. Regulates dendritic spine morphology.
CC Involved in calcium-dependent exocytosis. May play a role in
CC neurotransmitter release or synapse maintenance.
CC {ECO:0000269|PubMed:10625663, ECO:0000269|PubMed:19146815}.
CC -!- SUBUNIT: Interacts with BCAR1/p130Cas through its C-terminal domain and
CC with CSK, CTTN and SRC (By similarity). Also interacts with MAPRE3/EB3,
CC SORBS3/vinexin and the N-terminal coiled-coil region of SNAP25.
CC {ECO:0000250, ECO:0000269|PubMed:10625663, ECO:0000269|PubMed:18662323,
CC ECO:0000269|PubMed:19146815}.
CC -!- INTERACTION:
CC Q9QXY2; P60881: Snap25; NbExp=3; IntAct=EBI-1394088, EBI-1027214;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:22673903}. Cell projection, axon. Cell projection,
CC dendrite {ECO:0000269|PubMed:19146815}. Presynapse
CC {ECO:0000269|PubMed:18662323}. Postsynapse
CC {ECO:0000269|PubMed:18662323, ECO:0000269|PubMed:19146815}.
CC Postsynaptic density {ECO:0000269|PubMed:19146815}. Note=Localized to
CC the perinuclear region, lamellopodia, cortical actin and actin stress
CC fibers but not to focal adhesions. Strongly expressed in axons and
CC dendrites of the CA1 and CA3 hippocampal regions and of the dentate
CC gyrus. Detected in both presynapses and postsynapses and enriched in
CC postsynaptic density fractions. {ECO:0000269|PubMed:18662323,
CC ECO:0000269|PubMed:19146815, ECO:0000269|PubMed:22673903}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:10625663}; Synonyms=SNIP-b
CC {ECO:0000303|PubMed:10625663};
CC IsoId=Q9QXY2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10625663}; Synonyms=SNIP-a
CC {ECO:0000303|PubMed:10625663};
CC IsoId=Q9QXY2-2; Sequence=VSP_050633;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in brain. Abundant in
CC telencephalon and expressed moderately in cerebellum, hypothalamus,
CC thalamus, superior and inferior colliculi, and olfactory bulb. No
CC expression detected in medulla oblongata, spinal cord or pituitary
CC gland. Enriched in the neuropil rather than soma in the thalamus,
CC corpus striatum and cerebral cortex. Detected in astrocytes.
CC {ECO:0000269|PubMed:10625663, ECO:0000269|PubMed:18662323}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expression increases dramatically
CC between E14.5 and E18.5 (at protein level).
CC {ECO:0000269|PubMed:18662323}.
CC -!- PTM: Tyrosine-phosphorylated in response to EGF and to cell adhesion to
CC integrin ligands. {ECO:0000250|UniProtKB:Q9C0H9}.
CC -!- SIMILARITY: Belongs to the SRCIN1 family. {ECO:0000305}.
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DR EMBL; AF156981; AAF25003.1; -; mRNA.
DR EMBL; AF156982; AAF25004.1; -; mRNA.
DR RefSeq; NP_062251.1; NM_019378.1. [Q9QXY2-1]
DR AlphaFoldDB; Q9QXY2; -.
DR SMR; Q9QXY2; -.
DR BioGRID; 248555; 7.
DR IntAct; Q9QXY2; 7.
DR MINT; Q9QXY2; -.
DR STRING; 10116.ENSRNOP00000016070; -.
DR iPTMnet; Q9QXY2; -.
DR PhosphoSitePlus; Q9QXY2; -.
DR SwissPalm; Q9QXY2; -.
DR PaxDb; Q9QXY2; -.
DR PRIDE; Q9QXY2; -.
DR GeneID; 56029; -.
DR KEGG; rno:56029; -.
DR UCSC; RGD:708439; rat. [Q9QXY2-1]
DR CTD; 80725; -.
DR RGD; 708439; Srcin1.
DR VEuPathDB; HostDB:ENSRNOG00000011475; -.
DR eggNOG; ENOG502QPNH; Eukaryota.
DR HOGENOM; CLU_002507_0_0_1; -.
DR InParanoid; Q9QXY2; -.
DR OMA; FRMAPSS; -.
DR OrthoDB; 65773at2759; -.
DR PhylomeDB; Q9QXY2; -.
DR PRO; PR:Q9QXY2; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000011475; Expressed in frontal cortex and 17 other tissues.
DR Genevisible; Q9QXY2; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:RGD.
DR GO; GO:0050709; P:negative regulation of protein secretion; IMP:RGD.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR InterPro; IPR022782; AIP3-like_C.
DR InterPro; IPR026727; Srcin1.
DR PANTHER; PTHR22741:SF5; PTHR22741:SF5; 1.
DR Pfam; PF03915; AIP3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Exocytosis; Methylation; Phosphoprotein; Reference proteome;
KW Synapse.
FT CHAIN 1..1197
FT /note="SRC kinase signaling inhibitor 1"
FT /id="PRO_0000072013"
FT REGION 19..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..731
FT /note="Interaction with SNAP25"
FT /evidence="ECO:0000269|PubMed:10625663"
FT REGION 891..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 688..708
FT /evidence="ECO:0000255"
FT COILED 760..780
FT /evidence="ECO:0000255"
FT COMPBIAS 20..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..532
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1047
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0H9"
FT MOD_RES 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0H9"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0H9"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 276
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 364
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 371
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0H9"
FT MOD_RES 431
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 535
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 658
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 671
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 918
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0H9"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1077
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1094
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QWI6"
FT VAR_SEQ 1174..1197
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10625663"
FT /id="VSP_050633"
SQ SEQUENCE 1197 AA; 129744 MW; 8C9A2E630FB31C33 CRC64;
MQPWQCLRRF ALAWWERTAE GRARSPREEV GPRDPGGRGE PDPERSSPPM LSADDAEYPR
EYRTLGGGGS GGSGGRRFSN VGLVHTSERR HTVIAAQSLE ALSGLQKADA DRKRDAFMDH
LKSKYPQHAL ALRGQQDRMR EQQPNYWSFK TRSSRHTQGA QPGLADQAAK LSYASAESLE
TMSEAELPLG FSRMNRFRQS LPLSRSASQT KLRSPGVLFL QFGEETRRVH ITHEVSSLDT
LHALIAHMFP QKLTMGMLKS PNTAILIKDE ARNVFYELED VRDIQDRSII KIYRKEPLYA
AFPGSHLTNG DLRREMVYAS RESSPTRRLN NLSPASHLAS SSPPPGLPSG LPSGLPSGSP
SRSRLSYAGG RPPSYAGSPV HHAAERLGGA PTSQGVSPSP SAILERRDVK PDEDLAGKAG
GMVLVKGEGL YADPYGLLHE GRLSLAAAAG DPFAYPGAGG LYKRGSVRSL STYSAAALQS
DLEDSLYKAG AGGPLYGDGY GFRLPPSSPQ KLADVSAPSG GPPPPHSPYS GPPSRGSPVR
QSFRKDSGSS SVFAESPGGK ARSTGASTAG APPSELFPGP GERSLVGFGP PVPAKDTETR
ERMEAMEKQI ASLTGLVQSA LLRGSEPETP SEKIEGSNGA ATPSAPVCGS GSRSSGATPV
SGPPPPAVSS TPAGQPTAVS RLQMQMHLRG LQNSASDLRG QLQQLRKLQL QNQESVRALL
KRTEAELSMR VSEAARRQED PLQRQRTLVE EERLRYLNDE ELITQQLNDL EKSVEKIQRD
VAHNHRLVPG PELEEKALVL KQLGETLTEL KAHFPGLQSK MRVVLRVEVE AVKFLKEEPQ
RLDGLLKRCR VVTDTLAQIR RQVDEGVWPP PNNLLNQSPK KVAAETDFSK GLDFEIPPPS
PPLNLHELSG PAEGTPLTPK SGNPTKGLDA PSKRNMDKAV SVEAAERDWE EKRAALTQYS
AKDINRLLEE TQAELLKAIP DLDCASKTHP GPTPTPDHKP PKAPHGQKAA PRTEPSGRRG
SDELTVPRYR TEKPSKSPPP PPPRRSFPSS HGLTTTRTGE VVVTSKKDSV FIKKAESEEL
EIQKPQVKLR RAVSEVVRPA STPPIMASAI KDEDDEERII AELESGGGSV PPMKVVTPGA
SRLKAAQGPA GSPDKGKHGK QRTEYMRIQA QQQVRVGYQA PRPLEGCTPR LCYMPLS
