SMAP2_HUMAN
ID SMAP2_HUMAN Reviewed; 429 AA.
AC Q8WU79; B2R7T1; B7Z5B5; B7Z8V2; D3DPV2; Q5QPL2; Q96C93; Q9NST2; Q9UJL8;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Stromal membrane-associated protein 2;
DE AltName: Full=Stromal membrane-associated protein 1-like;
GN Name=SMAP2; Synonyms=SMAP1L;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RA Rhodes S., Huckle E.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Neutrophil, Thalamus, and Trachea;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell, and Colon;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-219; SER-223;
RP SER-225 AND SER-240, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-240, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-132 IN COMPLEX WITH ZINC IONS.
RG Structural genomics consortium (SGC);
RT "Structure of the GAP domain of SMAP1L (LOC64744) stromal membrane-
RT associated protein 1-like.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: GTPase activating protein that acts on ARF1. Can also
CC activate ARF6 (in vitro). May play a role in clathrin-dependent
CC retrograde transport from early endosomes to the trans-Golgi network
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ARF1. Interacts with PICALM and clathrin heavy
CC chains (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8WU79; O14503: BHLHE40; NbExp=3; IntAct=EBI-2822515, EBI-711810;
CC Q8WU79; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-2822515, EBI-946029;
CC Q8WU79; O43186: CRX; NbExp=3; IntAct=EBI-2822515, EBI-748171;
CC Q8WU79; O75553: DAB1; NbExp=3; IntAct=EBI-2822515, EBI-7875264;
CC Q8WU79; Q15038: DAZAP2; NbExp=6; IntAct=EBI-2822515, EBI-724310;
CC Q8WU79; Q92567: FAM168A; NbExp=3; IntAct=EBI-2822515, EBI-7957930;
CC Q8WU79; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-2822515, EBI-11962084;
CC Q8WU79; Q9Y5V3: MAGED1; NbExp=6; IntAct=EBI-2822515, EBI-716006;
CC Q8WU79; P35548: MSX2; NbExp=3; IntAct=EBI-2822515, EBI-6447480;
CC Q8WU79; Q8IYB5-2: SMAP1; NbExp=3; IntAct=EBI-2822515, EBI-12061577;
CC Q8WU79; Q96A09: TENT5B; NbExp=3; IntAct=EBI-2822515, EBI-752030;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Detected in multiple foci
CC throughout the cytoplasm and in juxtanuclear structures. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WU79-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WU79-2; Sequence=VSP_018504;
CC Name=3;
CC IsoId=Q8WU79-3; Sequence=VSP_043789;
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DR EMBL; AL133206; CAB61580.1; -; mRNA.
DR EMBL; AL137764; CAB70912.1; -; mRNA.
DR EMBL; AK298702; BAH12851.1; -; mRNA.
DR EMBL; AK303975; BAH14088.1; -; mRNA.
DR EMBL; AK313105; BAG35928.1; -; mRNA.
DR EMBL; AK316218; BAH14589.1; -; mRNA.
DR EMBL; AL031985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07220.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07222.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07221.1; -; Genomic_DNA.
DR EMBL; BC014512; AAH14512.1; -; mRNA.
DR EMBL; BC021133; AAH21133.1; -; mRNA.
DR CCDS; CCDS451.1; -. [Q8WU79-1]
DR CCDS; CCDS55592.1; -. [Q8WU79-2]
DR CCDS; CCDS55593.1; -. [Q8WU79-3]
DR RefSeq; NP_001185907.1; NM_001198978.1. [Q8WU79-2]
DR RefSeq; NP_001185908.1; NM_001198979.1.
DR RefSeq; NP_001185909.1; NM_001198980.1. [Q8WU79-3]
DR RefSeq; NP_073570.1; NM_022733.2. [Q8WU79-1]
DR PDB; 2IQJ; X-ray; 1.90 A; A/B=1-132.
DR PDBsum; 2IQJ; -.
DR AlphaFoldDB; Q8WU79; -.
DR SMR; Q8WU79; -.
DR BioGRID; 122260; 166.
DR IntAct; Q8WU79; 34.
DR MINT; Q8WU79; -.
DR STRING; 9606.ENSP00000361803; -.
DR GlyGen; Q8WU79; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q8WU79; -.
DR PhosphoSitePlus; Q8WU79; -.
DR BioMuta; SMAP2; -.
DR DMDM; 74760545; -.
DR EPD; Q8WU79; -.
DR jPOST; Q8WU79; -.
DR MassIVE; Q8WU79; -.
DR MaxQB; Q8WU79; -.
DR PaxDb; Q8WU79; -.
DR PeptideAtlas; Q8WU79; -.
DR PRIDE; Q8WU79; -.
DR ProteomicsDB; 74642; -. [Q8WU79-1]
DR ProteomicsDB; 74643; -. [Q8WU79-2]
DR ProteomicsDB; 74644; -. [Q8WU79-3]
DR Antibodypedia; 17974; 139 antibodies from 23 providers.
DR DNASU; 64744; -.
DR Ensembl; ENST00000372708.5; ENSP00000361793.1; ENSG00000084070.12. [Q8WU79-2]
DR Ensembl; ENST00000372718.8; ENSP00000361803.3; ENSG00000084070.12. [Q8WU79-1]
DR Ensembl; ENST00000539317.2; ENSP00000442835.1; ENSG00000084070.12. [Q8WU79-3]
DR GeneID; 64744; -.
DR KEGG; hsa:64744; -.
DR MANE-Select; ENST00000372718.8; ENSP00000361803.3; NM_022733.3; NP_073570.1.
DR UCSC; uc001cfj.4; human. [Q8WU79-1]
DR CTD; 64744; -.
DR DisGeNET; 64744; -.
DR GeneCards; SMAP2; -.
DR HGNC; HGNC:25082; SMAP2.
DR HPA; ENSG00000084070; Tissue enhanced (lymphoid).
DR neXtProt; NX_Q8WU79; -.
DR OpenTargets; ENSG00000084070; -.
DR PharmGKB; PA162403939; -.
DR VEuPathDB; HostDB:ENSG00000084070; -.
DR eggNOG; KOG0703; Eukaryota.
DR GeneTree; ENSGT00940000158387; -.
DR HOGENOM; CLU_023062_5_0_1; -.
DR InParanoid; Q8WU79; -.
DR OMA; MMGYGQS; -.
DR OrthoDB; 1097163at2759; -.
DR PhylomeDB; Q8WU79; -.
DR TreeFam; TF313876; -.
DR PathwayCommons; Q8WU79; -.
DR SignaLink; Q8WU79; -.
DR BioGRID-ORCS; 64744; 14 hits in 1029 CRISPR screens.
DR ChiTaRS; SMAP2; human.
DR EvolutionaryTrace; Q8WU79; -.
DR GenomeRNAi; 64744; -.
DR Pharos; Q8WU79; Tbio.
DR PRO; PR:Q8WU79; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8WU79; protein.
DR Bgee; ENSG00000084070; Expressed in blood and 165 other tissues.
DR ExpressionAtlas; Q8WU79; baseline and differential.
DR Genevisible; Q8WU79; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.220.150; -; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; GTPase activation;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..429
FT /note="Stromal membrane-associated protein 2"
FT /id="PRO_0000235841"
FT DOMAIN 13..137
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 28..51
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 138..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..232
FT /note="Interaction with clathrin heavy chains"
FT /evidence="ECO:0000250"
FT REGION 217..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..429
FT /note="Interaction with PICALM"
FT /evidence="ECO:0000250"
FT COMPBIAS 138..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..80
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043789"
FT VAR_SEQ 1..33
FT /note="MTGKSVKDVDRYQAVLANLLLEEDNKFCADCQS -> MIF (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_018504"
FT VARIANT 289
FT /note="A -> T (in dbSNP:rs34845213)"
FT /id="VAR_048327"
FT HELIX 13..19
FT /evidence="ECO:0007829|PDB:2IQJ"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:2IQJ"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:2IQJ"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:2IQJ"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:2IQJ"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2IQJ"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:2IQJ"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2IQJ"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2IQJ"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2IQJ"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:2IQJ"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:2IQJ"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2IQJ"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:2IQJ"
SQ SEQUENCE 429 AA; 46786 MW; C2787BECAE37D6BD CRC64;
MTGKSVKDVD RYQAVLANLL LEEDNKFCAD CQSKGPRWAS WNIGVFICIR CAGIHRNLGV
HISRVKSVNL DQWTQEQIQC MQEMGNGKAN RLYEAYLPET FRRPQIDPAV EGFIRDKYEK
KKYMDRSLDI NAFRKEKDDK WKRGSEPVPE KKLEPVVFEK VKMPQKKEDP QLPRKSSPKS
TAPVMDLLGL DAPVACSIAN SKTSNTLEKD LDLLASVPSP SSSGSRKVVG SMPTAGSAGS
VPENLNLFPE PGSKSEEIGK KQLSKDSILS LYGSQTPQMP TQAMFMAPAQ MAYPTAYPSF
PGVTPPNSIM GSMMPPPVGM VAQPGASGMV APMAMPAGYM GGMQASMMGV PNGMMTTQQA
GYMAGMAAMP QTVYGVQPAQ QLQWNLTQMT QQMAGMNFYG ANGMMNYGQS MSGGNGQAAN
QTLSPQMWK
