ID   SLAP1_RAT               Reviewed;         312 AA.
AC   P59622;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Src-like-adapter;
DE   AltName: Full=Src-like-adapter protein 1;
DE            Short=SLAP-1;
GN   Name=Sla; Synonyms=Slap, Slap1;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Alifragis P., Molnar Z., Parnavelas J.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND IDENTIFICATION BY
RP   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: Adapter protein, which negatively regulates T-cell receptor
CC       (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of
CC       nuclear factor of activated T-cells. Involved in the negative
CC       regulation of positive selection and mitosis of T-cells. May act by
CC       linking signaling proteins such as ZAP70 with CBL, leading to a CBL
CC       dependent degradation of signaling proteins (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with phosphorylated CBL, SYK and LAT.
CC       Homodimerization and interaction with phosphorylated CBL occurs via its
CC       C-terminal domain. Interacts with PDGFRB and EPHA2. Interacts with
CC       phosphorylated proteins ZAP70; CD3Z; VAV1 and LCP2 via its SH2 domain
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}.
CC       Note=Colocalizes with endosomes. {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal domain is essential for the homodimerization and
CC       the interaction with CBL. While the interaction with CBL is apparently
CC       mediated via the hydrophobic region of this domain, the highly charged
CC       region is apparently required for the homodimerization (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
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DR   EMBL; AY217759; AAO61134.1; -; mRNA.
DR   RefSeq; NP_835198.1; NM_178097.2.
DR   AlphaFoldDB; P59622; -.
DR   SMR; P59622; -.
DR   IntAct; P59622; 2.
DR   STRING; 10116.ENSRNOP00000007982; -.
DR   iPTMnet; P59622; -.
DR   PhosphoSitePlus; P59622; -.
DR   PaxDb; P59622; -.
DR   PRIDE; P59622; -.
DR   GeneID; 338477; -.
DR   KEGG; rno:338477; -.
DR   UCSC; RGD:631373; rat.
DR   CTD; 6503; -.
DR   RGD; 631373; Sla.
DR   eggNOG; ENOG502QPWY; Eukaryota.
DR   InParanoid; P59622; -.
DR   OrthoDB; 1051480at2759; -.
DR   PhylomeDB; P59622; -.
DR   Reactome; R-RNO-9706369; Negative regulation of FLT3.
DR   PRO; PR:P59622; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd10344; SH2_SLAP; 1.
DR   CDD; cd12010; SH3_SLAP; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR035055; SLAP.
DR   InterPro; IPR035052; SLAP_SH2.
DR   InterPro; IPR035596; SLAP_SH3.
DR   PANTHER; PTHR24418:SF293; PTHR24418:SF293; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endosome; Phosphoprotein; Reference proteome; SH2 domain;
KW   SH3 domain.
FT   CHAIN           1..312
FT                   /note="Src-like-adapter"
FT                   /id="PRO_0000071948"
FT   DOMAIN          38..98
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          100..191
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..312
FT                   /note="SLA C-terminal"
FT   MOD_RES         274
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   312 AA;  34745 MW;  A05412D39AE68388 CRC64;
     MLCRLPGPST SRGEKEMGNS MKSTPAPLER PLSNTEGLES DFLAVLNDYP SPDISPPIFR
     RGEKLRVISD EGGWWKAISL STGRESYIPG ICVARVYHGW LFEGLGRDKA EELLQLPDTK
     IGSFMIRESE TKKGFYSLSV RHRQVKHYRI FRLPNNWYYI SPRLTFQCLE DLVTHYSEVA
     DGLCCVLTTP CLAQNTPAPT AQPSPCTSPG SPVTLRQKTF DWKRVSSLQE GPEGAENPLR
     VDESLFSYGL RESIASYLSL TGDDSSNFDR KKKSLSLIYS GSKRKSSFFS APNTLKINAL
     AGTQKTKALT AT