SLAP2_HUMAN
ID SLAP2_HUMAN Reviewed; 261 AA.
AC Q9H6Q3; A8K648; E1P5U1; E1P5U2; Q5TH27; Q5TH28; Q8WY18; Q96QI4; Q9H135;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Src-like-adapter 2;
DE AltName: Full=Modulator of antigen receptor signaling;
DE Short=MARS;
DE AltName: Full=Src-like adapter protein 2;
DE Short=SLAP-2;
GN Name=SLA2; Synonyms=C20orf156, SLAP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1), CHARACTERIZATION, FUNCTION, MYRISTOYLATION
RP AT GLY-2, INTERACTION WITH CBL, AND MUTAGENESIS OF GLY-2.
RX PubMed=11696592; DOI=10.1084/jem.194.9.1263;
RA Holland S.J., Liao X.C., Mendenhall M.K., Zhou X., Pardo J., Chu P.,
RA Spencer C., Fu A.C., Sheng N., Yu P., Pali E., Nagin A., Shen M., Yu S.,
RA Chan E., Wu X., Li C., Woisetschlager M., Aversa G., Kolbinger F.,
RA Bennett M.K., Molineaux S., Luo Y., Payan D.G., Mancebo H.S.Y., Wu J.;
RT "Functional cloning of Src-like adapter protein-2 (SLAP-2), a novel
RT inhibitor of antigen receptor signaling.";
RL J. Exp. Med. 194:1263-1276(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 3 AND 4), AND ALTERNATIVE INITIATION.
RC TISSUE=Thymus;
RX PubMed=12527895; DOI=10.1038/sj.onc.1206114;
RA Loreto M.P., McGlade C.J.;
RT "Cloning and characterization of human Src-like adaptor protein 2 and a
RT novel splice isoform, SLAP-2-v.";
RL Oncogene 22:266-273(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hepatoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP CHARACTERIZATION.
RX PubMed=11891219; DOI=10.1074/jbc.m110318200;
RA Pandey A., Ibarrola N., Kratchmarova I., Fernandez M.M.,
RA Constantinescu S.N., Ohara O., Sawasdikosol S., Lodish H.F., Mann M.;
RT "A novel Src homology 2 domain-containing molecule, Src-like adapter
RT protein-2 (SLAP-2), which negatively regulates T cell receptor signaling.";
RL J. Biol. Chem. 277:19131-19138(2002).
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. May act by linking signaling
CC proteins such as ZAP70 with CBL, leading to a CBL dependent degradation
CC of signaling proteins. {ECO:0000269|PubMed:11696592}.
CC -!- SUBUNIT: Interacts (via SH2 domain) with ZAP70 (phosphorylated) and
CC CD3Z (phosphorylated). Interacts (via SH2 domain) with CSF1R
CC (phosphorylated) (By similarity). Interacts (via its C-terminal domain)
CC with CBL (phosphorylated). {ECO:0000250, ECO:0000269|PubMed:11696592}.
CC -!- INTERACTION:
CC Q9H6Q3; P04626: ERBB2; NbExp=2; IntAct=EBI-1222854, EBI-641062;
CC Q9H6Q3; Q13480: GAB1; NbExp=4; IntAct=EBI-1222854, EBI-517684;
CC Q9H6Q3; P10721: KIT; NbExp=2; IntAct=EBI-1222854, EBI-1379503;
CC Q9H6Q3; P08581: MET; NbExp=4; IntAct=EBI-1222854, EBI-1039152;
CC Q9H6Q3; P54646: PRKAA2; NbExp=3; IntAct=EBI-1222854, EBI-1383852;
CC Q9H6Q3; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-1222854, EBI-7353612;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane. Cytoplasmic vesicle.
CC Note=Localized to the plasma membrane and intracellular vesicles,
CC including late endosomal vesicles.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}. Note=May be
CC cytoplasmic and is not localized to membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=1; Synonyms=p28;
CC IsoId=Q9H6Q3-1; Sequence=Displayed;
CC Name=2; Synonyms=p23, SLAP-2-v, MARS-v;
CC IsoId=Q9H6Q3-2; Sequence=VSP_007240, VSP_007241;
CC Name=3; Synonyms=p25;
CC IsoId=Q9H6Q3-3; Sequence=VSP_018794;
CC Name=4; Synonyms=p20;
CC IsoId=Q9H6Q3-4; Sequence=VSP_018794, VSP_007240, VSP_007241;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in immune system, with
CC highest levels in peripheral blood leukocytes. Expressed in spleen,
CC thymus and lymph nodes. Expressed in T-cells as well as in monocytes,
CC and at low level in B-cells. Also detected in placenta, prostate, skin,
CC retina and colon.
CC -!- DOMAIN: The loss of the C-terminal domain partially abolishes the
CC inhibitory function, but can be partially compensated by higher level
CC of protein expression.
CC -!- PTM: Phosphorylated by CSF1R. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation at Met-
CC 28 of isoform 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative initiation at Met-
CC 28 of isoform 2. {ECO:0000305}.
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DR EMBL; AF326353; AAL29204.1; -; mRNA.
DR EMBL; AF290985; AAL38197.1; -; mRNA.
DR EMBL; AF290986; AAL38198.1; -; mRNA.
DR EMBL; AK025645; BAB15201.1; -; mRNA.
DR EMBL; AK291513; BAF84202.1; -; mRNA.
DR EMBL; AL031662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL050318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76116.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76117.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76118.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76119.1; -; Genomic_DNA.
DR EMBL; BC042041; AAH42041.1; -; mRNA.
DR CCDS; CCDS13282.1; -. [Q9H6Q3-1]
DR CCDS; CCDS13283.1; -. [Q9H6Q3-2]
DR RefSeq; NP_115590.1; NM_032214.3. [Q9H6Q3-1]
DR RefSeq; NP_778252.1; NM_175077.2. [Q9H6Q3-2]
DR PDB; 4M4Z; X-ray; 2.10 A; A=29-193.
DR PDBsum; 4M4Z; -.
DR AlphaFoldDB; Q9H6Q3; -.
DR SMR; Q9H6Q3; -.
DR BioGRID; 123928; 30.
DR ELM; Q9H6Q3; -.
DR IntAct; Q9H6Q3; 10.
DR MINT; Q9H6Q3; -.
DR STRING; 9606.ENSP00000262866; -.
DR iPTMnet; Q9H6Q3; -.
DR PhosphoSitePlus; Q9H6Q3; -.
DR BioMuta; SLA2; -.
DR DMDM; 30173374; -.
DR jPOST; Q9H6Q3; -.
DR MassIVE; Q9H6Q3; -.
DR MaxQB; Q9H6Q3; -.
DR PaxDb; Q9H6Q3; -.
DR PeptideAtlas; Q9H6Q3; -.
DR PRIDE; Q9H6Q3; -.
DR ProteomicsDB; 81005; -. [Q9H6Q3-1]
DR ProteomicsDB; 81006; -. [Q9H6Q3-2]
DR ProteomicsDB; 81007; -. [Q9H6Q3-3]
DR ProteomicsDB; 81008; -. [Q9H6Q3-4]
DR Antibodypedia; 26550; 446 antibodies from 23 providers.
DR DNASU; 84174; -.
DR Ensembl; ENST00000262866.9; ENSP00000262866.4; ENSG00000101082.14. [Q9H6Q3-1]
DR Ensembl; ENST00000360672.2; ENSP00000353890.2; ENSG00000101082.14. [Q9H6Q3-2]
DR GeneID; 84174; -.
DR KEGG; hsa:84174; -.
DR MANE-Select; ENST00000262866.9; ENSP00000262866.4; NM_032214.4; NP_115590.1.
DR UCSC; uc002xfu.4; human. [Q9H6Q3-1]
DR CTD; 84174; -.
DR DisGeNET; 84174; -.
DR GeneCards; SLA2; -.
DR HGNC; HGNC:17329; SLA2.
DR HPA; ENSG00000101082; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 606577; gene.
DR neXtProt; NX_Q9H6Q3; -.
DR OpenTargets; ENSG00000101082; -.
DR PharmGKB; PA38231; -.
DR VEuPathDB; HostDB:ENSG00000101082; -.
DR eggNOG; ENOG502QPJN; Eukaryota.
DR GeneTree; ENSGT00940000160331; -.
DR HOGENOM; CLU_084503_1_0_1; -.
DR InParanoid; Q9H6Q3; -.
DR OMA; QSRRGCY; -.
DR OrthoDB; 1051480at2759; -.
DR PhylomeDB; Q9H6Q3; -.
DR TreeFam; TF354288; -.
DR PathwayCommons; Q9H6Q3; -.
DR Reactome; R-HSA-9706369; Negative regulation of FLT3.
DR SignaLink; Q9H6Q3; -.
DR SIGNOR; Q9H6Q3; -.
DR BioGRID-ORCS; 84174; 10 hits in 1068 CRISPR screens.
DR ChiTaRS; SLA2; human.
DR GeneWiki; SLA2; -.
DR GenomeRNAi; 84174; -.
DR Pharos; Q9H6Q3; Tbio.
DR PRO; PR:Q9H6Q3; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H6Q3; protein.
DR Bgee; ENSG00000101082; Expressed in buccal mucosa cell and 124 other tissues.
DR Genevisible; Q9H6Q3; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; NAS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
DR GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IBA:GO_Central.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0035591; F:signaling adaptor activity; IDA:UniProtKB.
DR GO; GO:0050851; P:antigen receptor-mediated signaling pathway; TAS:UniProtKB.
DR GO; GO:0019724; P:B cell mediated immunity; TAS:UniProtKB.
DR GO; GO:0050849; P:negative regulation of calcium-mediated signaling; IDA:UniProtKB.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; NAS:UniProtKB.
DR GO; GO:0042110; P:T cell activation; IDA:UniProtKB.
DR CDD; cd10344; SH2_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; IPR035054; SLAP2.
DR InterPro; IPR035052; SLAP_SH2.
DR PANTHER; PTHR10155:SF6; PTHR10155:SF6; 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 3D-structure; Alternative initiation; Alternative splicing; Cell membrane;
KW Cytoplasm; Cytoplasmic vesicle; Lipoprotein; Membrane; Myristate;
KW Phosphoprotein; Reference proteome; SH2 domain; SH3 domain.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..261
FT /note="Src-like-adapter 2"
FT /id="PRO_0000022351"
FT DOMAIN 32..92
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 94..191
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..261
FT /note="SLA C-terminal"
FT COMPBIAS 6..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:11696592"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_018794"
FT VAR_SEQ 179..210
FT /note="LADDICCLLKEPCVLQRAGPLPGKDIPLPVTV -> GWPAPWQGYTPTCDCA
FT EDTTQLERAGQLPPVF (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_007240"
FT VAR_SEQ 211..261
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_007241"
FT VARIANT 210
FT /note="V -> M (in dbSNP:rs34834764)"
FT /id="VAR_051361"
FT MUTAGEN 2
FT /note="G->A: Abolishes localization to membranes."
FT /evidence="ECO:0000269|PubMed:11696592"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:4M4Z"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:4M4Z"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:4M4Z"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:4M4Z"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:4M4Z"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:4M4Z"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:4M4Z"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:4M4Z"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:4M4Z"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:4M4Z"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:4M4Z"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:4M4Z"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:4M4Z"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:4M4Z"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:4M4Z"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:4M4Z"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:4M4Z"
SQ SEQUENCE 261 AA; 28585 MW; 858AF03451672B3D CRC64;
MGSLPSRRKS LPSPSLSSSV QGQGPVTMEA ERSKATAVAL GSFPAGGPAE LSLRLGEPLT
IVSEDGDWWT VLSEVSGREY NIPSVHVAKV SHGWLYEGLS REKAEELLLL PGNPGGAFLI
RESQTRRGSY SLSVRLSRPA SWDRIRHYRI HCLDNGWLYI SPRLTFPSLQ ALVDHYSELA
DDICCLLKEP CVLQRAGPLP GKDIPLPVTV QRTPLNWKEL DSSLLFSEAA TGEESLLSEG
LRESLSFYIS LNDEAVSLDD A
