ID SMAP1_HUMAN Reviewed; 467 AA.
AC Q8IYB5; Q53H70; Q5SYQ2; Q6PK24; Q8NDH4; Q96L38; Q96L39; Q9H8X4;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 27-MAR-2024, entry version 169.
DE RecName: Full=Stromal membrane-associated protein 1;
GN Name=SMAP1;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Blood, and Bone marrow;
RX PubMed=12119110; DOI=10.1016/s0378-1119(02)00645-5;
RA Marcos I., Borrego S., Rodriguez de Cordoba S., Galan J.J., Antinolo G.;
RT "Cloning, characterization and chromosome mapping of the human SMAP1
RT gene.";
RL Gene 292:167-171(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 MRNA].
RC TISSUE=Brain;
RA Guo J.H., Zan Q., Yu L.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT VAL-212.
RC TISSUE=Colon;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Ovary;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 248-467.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
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 [9]
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 [10]
RP STRUCTURE BY NMR OF 9-136 IN COMPLEX WITH ZINC IONS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of ARFGAP domain from human SMAP1.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: GTPase activating protein that acts on ARF6. Plays a role in
CC clathrin-dependent endocytosis. May play a role in erythropoiesis (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ARF6. Interacts with clathrin heavy chains via
CC the clathrin box-like motif (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8IYB5-2; Q9NZN9: AIPL1; NbExp=3; IntAct=EBI-12061577, EBI-6557414;
CC Q8IYB5-2; O43186: CRX; NbExp=3; IntAct=EBI-12061577, EBI-748171;
CC Q8IYB5-2; Q13952-2: NFYC; NbExp=3; IntAct=EBI-12061577, EBI-11956831;
CC Q8IYB5-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12061577, EBI-741158;
CC Q8IYB5-2; Q99471: PFDN5; NbExp=3; IntAct=EBI-12061577, EBI-357275;
CC Q8IYB5-2; P86480: PRR20D; NbExp=6; IntAct=EBI-12061577, EBI-12754095;
CC Q8IYB5-2; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-12061577, EBI-2798044;
CC Q8IYB5-2; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-12061577, EBI-740343;
CC Q8IYB5-2; Q8WU79: SMAP2; NbExp=3; IntAct=EBI-12061577, EBI-2822515;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=SMAP1A;
CC IsoId=Q8IYB5-1; Sequence=Displayed;
CC Name=2; Synonyms=SMAP1B;
CC IsoId=Q8IYB5-2; Sequence=VSP_018502;
CC Name=3;
CC IsoId=Q8IYB5-3; Sequence=VSP_018502, VSP_018503;
CC -!- TISSUE SPECIFICITY: Detected in bone marrow, adrenal gland, trachea,
CC lymph node, spinal cord, peripheral blood leukocytes, thyroid and
CC stomach. {ECO:0000269|PubMed:12119110}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08672.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/42974/SMAP1";
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DR EMBL; AY055003; AAL14714.1; -; mRNA.
DR EMBL; AY055004; AAL14715.1; -; mRNA.
DR EMBL; AY055015; AAL14716.1; -; Genomic_DNA.
DR EMBL; AY055005; AAL14716.1; JOINED; Genomic_DNA.
DR EMBL; AY055006; AAL14716.1; JOINED; Genomic_DNA.
DR EMBL; AY055007; AAL14716.1; JOINED; Genomic_DNA.
DR EMBL; AY055008; AAL14716.1; JOINED; Genomic_DNA.
DR EMBL; AY055009; AAL14716.1; JOINED; Genomic_DNA.
DR EMBL; AY055010; AAL14716.1; JOINED; Genomic_DNA.
DR EMBL; AY055011; AAL14716.1; JOINED; Genomic_DNA.
DR EMBL; AY055012; AAL14716.1; JOINED; Genomic_DNA.
DR EMBL; AY055013; AAL14716.1; JOINED; Genomic_DNA.
DR EMBL; AY055014; AAL14716.1; JOINED; Genomic_DNA.
DR EMBL; AY055015; AAL14717.1; -; Genomic_DNA.
DR EMBL; AY055005; AAL14717.1; JOINED; Genomic_DNA.
DR EMBL; AY055006; AAL14717.1; JOINED; Genomic_DNA.
DR EMBL; AY055007; AAL14717.1; JOINED; Genomic_DNA.
DR EMBL; AY055008; AAL14717.1; JOINED; Genomic_DNA.
DR EMBL; AY055010; AAL14717.1; JOINED; Genomic_DNA.
DR EMBL; AY055011; AAL14717.1; JOINED; Genomic_DNA.
DR EMBL; AY055012; AAL14717.1; JOINED; Genomic_DNA.
DR EMBL; AY055013; AAL14717.1; JOINED; Genomic_DNA.
DR EMBL; AY055014; AAL14717.1; JOINED; Genomic_DNA.
DR EMBL; AK023221; BAB14473.1; -; mRNA.
DR EMBL; AF442495; AAP97320.1; -; mRNA.
DR EMBL; AK222711; BAD96431.1; -; mRNA.
DR EMBL; AL354943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008672; AAH08672.1; ALT_SEQ; mRNA.
DR EMBL; BC028074; AAH28074.1; -; mRNA.
DR EMBL; BC036123; AAH36123.1; -; mRNA.
DR EMBL; AL833906; CAD38762.1; -; mRNA.
DR CCDS; CCDS43478.1; -. [Q8IYB5-1]
DR CCDS; CCDS4973.1; -. [Q8IYB5-2]
DR CCDS; CCDS64459.1; -. [Q8IYB5-3]
DR RefSeq; NP_001037770.1; NM_001044305.2. [Q8IYB5-1]
DR RefSeq; NP_001268368.1; NM_001281439.1. [Q8IYB5-3]
DR RefSeq; NP_001268369.1; NM_001281440.1.
DR RefSeq; NP_068759.2; NM_021940.4. [Q8IYB5-2]
DR PDB; 2CRR; NMR; -; A=9-136.
DR PDBsum; 2CRR; -.
DR AlphaFoldDB; Q8IYB5; -.
DR SMR; Q8IYB5; -.
DR BioGRID; 121956; 59.
DR IntAct; Q8IYB5; 22.
DR MINT; Q8IYB5; -.
DR STRING; 9606.ENSP00000359484; -.
DR GlyGen; Q8IYB5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IYB5; -.
DR PhosphoSitePlus; Q8IYB5; -.
DR BioMuta; SMAP1; -.
DR DMDM; 97190718; -.
DR EPD; Q8IYB5; -.
DR jPOST; Q8IYB5; -.
DR MassIVE; Q8IYB5; -.
DR MaxQB; Q8IYB5; -.
DR PaxDb; 9606-ENSP00000359484; -.
DR PeptideAtlas; Q8IYB5; -.
DR ProteomicsDB; 71145; -. [Q8IYB5-1]
DR ProteomicsDB; 71146; -. [Q8IYB5-2]
DR ProteomicsDB; 71147; -. [Q8IYB5-3]
DR Pumba; Q8IYB5; -.
DR Antibodypedia; 31248; 163 antibodies from 24 providers.
DR DNASU; 60682; -.
DR Ensembl; ENST00000316999.9; ENSP00000313382.5; ENSG00000112305.15. [Q8IYB5-2]
DR Ensembl; ENST00000370452.7; ENSP00000359481.3; ENSG00000112305.15. [Q8IYB5-3]
DR Ensembl; ENST00000370455.8; ENSP00000359484.3; ENSG00000112305.15. [Q8IYB5-1]
DR GeneID; 60682; -.
DR KEGG; hsa:60682; -.
DR MANE-Select; ENST00000370455.8; ENSP00000359484.3; NM_001044305.3; NP_001037770.1.
DR UCSC; uc003pfr.5; human. [Q8IYB5-1]
DR AGR; HGNC:19651; -.
DR CTD; 60682; -.
DR DisGeNET; 60682; -.
DR GeneCards; SMAP1; -.
DR HGNC; HGNC:19651; SMAP1.
DR HPA; ENSG00000112305; Low tissue specificity.
DR MIM; 611372; gene.
DR neXtProt; NX_Q8IYB5; -.
DR OpenTargets; ENSG00000112305; -.
DR PharmGKB; PA134893764; -.
DR VEuPathDB; HostDB:ENSG00000112305; -.
DR eggNOG; KOG0703; Eukaryota.
DR GeneTree; ENSGT00940000155884; -.
DR HOGENOM; CLU_023062_5_0_1; -.
DR InParanoid; Q8IYB5; -.
DR OMA; NNGWSGM; -.
DR OrthoDB; 1022106at2759; -.
DR PhylomeDB; Q8IYB5; -.
DR TreeFam; TF313876; -.
DR PathwayCommons; Q8IYB5; -.
DR SignaLink; Q8IYB5; -.
DR BioGRID-ORCS; 60682; 6 hits in 1151 CRISPR screens.
DR ChiTaRS; SMAP1; human.
DR EvolutionaryTrace; Q8IYB5; -.
DR GeneWiki; SMAP1; -.
DR GenomeRNAi; 60682; -.
DR Pharos; Q8IYB5; Tbio.
DR PRO; PR:Q8IYB5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8IYB5; Protein.
DR Bgee; ENSG00000112305; Expressed in cortical plate and 214 other cell types or tissues.
DR ExpressionAtlas; Q8IYB5; baseline and differential.
DR Genevisible; Q8IYB5; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030276; F:clathrin binding; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IBA:GO_Central.
DR CDD; cd08839; ArfGap_SMAP; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR044732; ArfGAP_SMAP1-like.
DR PANTHER; PTHR45705; FI20236P1; 1.
DR PANTHER; PTHR45705:SF8; STROMAL MEMBRANE-ASSOCIATED PROTEIN 1; 1.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; GTPase activation;
KW Membrane; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..467
FT /note="Stromal membrane-associated protein 1"
FT /id="PRO_0000235838"
FT DOMAIN 18..136
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 33..56
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 145..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 218..222
FT /note="Interaction with clathrin heavy chains"
FT /evidence="ECO:0000250"
FT COMPBIAS 160..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 139..165
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12119110,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.4"
FT /id="VSP_018502"
FT VAR_SEQ 424..467
FT /note="MNQQMAGMSISSATPTAGFGQPSSTTAGWSGSSSGQTLSTQLWK -> IMQK
FT GDAVLQHSISAIYWPMTRWLKCPLVDESADGWHEYQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_018503"
FT VARIANT 212
FT /note="A -> V (in dbSNP:rs2273566)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_048326"
FT CONFLICT 394
FT /note="P -> H (in Ref. 6; AAH36123)"
FT /evidence="ECO:0000305"
FT TURN 10..15
FT /evidence="ECO:0007829|PDB:2CRR"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:2CRR"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:2CRR"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2CRR"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2CRR"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:2CRR"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:2CRR"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2CRR"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2CRR"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:2CRR"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:2CRR"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:2CRR"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:2CRR"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:2CRR"
SQ SEQUENCE 467 AA; 50386 MW; 75935CB6F9F99DA9 CRC64;
MATRSCREKA QKLNEQHQLI LSKLLREEDN KYCADCEAKG PRWASWNIGV FICIRCAGIH
RNLGVHISRV KSVNLDQWTA EQIQCMQDMG NTKARLLYEA NLPENFRRPQ TDQAVEFFIR
DKYEKKKYYD KNAIAITNIS SSDAPLQPLV SSPSLQAAVD KNKLEKEKEK KKEEKKREKE
PEKPAKPLTA EKLQKKDQQL EPKKSTSPKK AAEPTVDLLG LDGPAVAPVT NGNTTVPPLN
DDLDIFGPMI SNPLPATVMP PAQGTPSAPA AATLSTVTSG DLDLFTEQTT KSEEVAKKQL
SKDSILSLYG TGTIQQQSTP GVFMGPTNIP FTSQAPAAFQ GFPSMGVPVP AAPGLIGNVM
GQSPSMMVGM PMPNGFMGNA QTGVMPLPQN VVGPQGGMVG QMGAPQSKFG LPQAQQPQWS
LSQMNQQMAG MSISSATPTA GFGQPSSTTA GWSGSSSGQT LSTQLWK
//
