ID   STRBP_HUMAN             Reviewed;         672 AA.
AC   Q96SI9; Q32NB9; Q9BUE1; Q9BXG4; Q9H0B4; Q9H7V1; Q9NUK4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=Spermatid perinuclear RNA-binding protein;
GN   Name=STRBP; Synonyms=SPNR;
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 [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RA   Sha J.H., Zhou Z.M., Li J.M.;
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta, and Retinoblastoma;
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=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Leiomyosarcoma, Retinoblastoma, and Uterus;
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].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [7]
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [10]
RP   STRUCTURE BY NMR OF 378-461.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of DSRM domain in spermatid perinuclear RNA-binding
RT   protein.";
RL   Submitted (OCT-2006) to the PDB data bank.
RN   [11]
RP   VARIANT [LARGE SCALE ANALYSIS] ARG-280.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Involved in spermatogenesis and sperm function. Plays a role
CC       in regulation of cell growth. Binds to double-stranded DNA and RNA.
CC       Binds most efficiently to poly(I:C) RNA than to poly(dI:dC) DNA. Binds
CC       also to single-stranded poly(G) RNA. Binds non-specifically to the mRNA
CC       PRM1 3'-UTR and adenovirus VA RNA (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with EIF2AK2. Associates with microtubules; it is
CC       unsure whether such interaction is direct or indirect. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q96SI9; P78563-4: ADARB1; NbExp=3; IntAct=EBI-740355, EBI-12002366;
CC       Q96SI9; Q13555-5: CAMK2G; NbExp=3; IntAct=EBI-740355, EBI-12020154;
CC       Q96SI9; O75553: DAB1; NbExp=3; IntAct=EBI-740355, EBI-7875264;
CC       Q96SI9; Q9UGU5: HMGXB4; NbExp=3; IntAct=EBI-740355, EBI-7261162;
CC       Q96SI9; O75569: PRKRA; NbExp=3; IntAct=EBI-740355, EBI-713955;
CC       Q96SI9; Q9NWB1-5: RBFOX1; NbExp=3; IntAct=EBI-740355, EBI-12123390;
CC       Q96SI9; Q93062: RBPMS; NbExp=4; IntAct=EBI-740355, EBI-740322;
CC       Q96SI9; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-740355, EBI-740343;
CC       Q96SI9; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-740355, EBI-11987469;
CC       Q96SI9; O95793: STAU1; NbExp=3; IntAct=EBI-740355, EBI-358174;
CC       Q96SI9; Q15633: TARBP2; NbExp=3; IntAct=EBI-740355, EBI-978581;
CC       Q96SI9; Q9NVV9: THAP1; NbExp=7; IntAct=EBI-740355, EBI-741515;
CC       Q96SI9; Q9H898-2: ZMAT4; NbExp=3; IntAct=EBI-740355, EBI-11529334;
CC       Q96SI9; Q9UL40: ZNF346; NbExp=3; IntAct=EBI-740355, EBI-2462313;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Microtubule-
CC       associated that localizes to the manchette in developing spermatids.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96SI9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96SI9-2; Sequence=VSP_022937;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI08732.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=BAA92120.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB14873.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF333337; AAK20832.1; -; mRNA.
DR   EMBL; AL136866; CAB66800.1; -; mRNA.
DR   EMBL; AK002169; BAA92120.1; ALT_INIT; mRNA.
DR   EMBL; AK024285; BAB14873.1; ALT_INIT; mRNA.
DR   EMBL; AK027890; BAB55434.1; -; mRNA.
DR   EMBL; AL365338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002693; AAH02693.2; -; mRNA.
DR   EMBL; BC017732; AAH17732.1; -; mRNA.
DR   EMBL; BC108731; AAI08732.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS55337.1; -. [Q96SI9-2]
DR   CCDS; CCDS6851.1; -. [Q96SI9-1]
DR   RefSeq; NP_001164608.1; NM_001171137.1. [Q96SI9-2]
DR   RefSeq; NP_060857.2; NM_018387.4. [Q96SI9-1]
DR   RefSeq; XP_016870383.1; XM_017014894.1.
DR   RefSeq; XP_016870384.1; XM_017014895.1.
DR   RefSeq; XP_016870385.1; XM_017014896.1.
DR   PDB; 2DMY; NMR; -; A=378-461.
DR   PDBsum; 2DMY; -.
DR   AlphaFoldDB; Q96SI9; -.
DR   SMR; Q96SI9; -.
DR   BioGRID; 120623; 285.
DR   IntAct; Q96SI9; 78.
DR   MINT; Q96SI9; -.
DR   STRING; 9606.ENSP00000321347; -.
DR   GlyGen; Q96SI9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96SI9; -.
DR   MetOSite; Q96SI9; -.
DR   PhosphoSitePlus; Q96SI9; -.
DR   SwissPalm; Q96SI9; -.
DR   BioMuta; STRBP; -.
DR   DMDM; 74752134; -.
DR   EPD; Q96SI9; -.
DR   jPOST; Q96SI9; -.
DR   MassIVE; Q96SI9; -.
DR   MaxQB; Q96SI9; -.
DR   PaxDb; 9606-ENSP00000415968; -.
DR   PeptideAtlas; Q96SI9; -.
DR   ProteomicsDB; 78115; -. [Q96SI9-1]
DR   ProteomicsDB; 78116; -. [Q96SI9-2]
DR   Pumba; Q96SI9; -.
DR   Antibodypedia; 16209; 89 antibodies from 21 providers.
DR   DNASU; 55342; -.
DR   Ensembl; ENST00000348403.10; ENSP00000321347.7; ENSG00000165209.19. [Q96SI9-1]
DR   Ensembl; ENST00000360998.3; ENSP00000354271.3; ENSG00000165209.19. [Q96SI9-2]
DR   Ensembl; ENST00000447404.6; ENSP00000415968.2; ENSG00000165209.19. [Q96SI9-1]
DR   GeneID; 55342; -.
DR   KEGG; hsa:55342; -.
DR   MANE-Select; ENST00000348403.10; ENSP00000321347.7; NM_018387.5; NP_060857.2.
DR   UCSC; uc004bnu.4; human. [Q96SI9-1]
DR   AGR; HGNC:16462; -.
DR   CTD; 55342; -.
DR   DisGeNET; 55342; -.
DR   GeneCards; STRBP; -.
DR   HGNC; HGNC:16462; STRBP.
DR   HPA; ENSG00000165209; Low tissue specificity.
DR   MIM; 611138; gene.
DR   neXtProt; NX_Q96SI9; -.
DR   OpenTargets; ENSG00000165209; -.
DR   PharmGKB; PA38145; -.
DR   VEuPathDB; HostDB:ENSG00000165209; -.
DR   eggNOG; KOG3792; Eukaryota.
DR   GeneTree; ENSGT00940000154687; -.
DR   HOGENOM; CLU_015490_1_0_1; -.
DR   InParanoid; Q96SI9; -.
DR   OMA; APLKGWX; -.
DR   OrthoDB; 4565640at2759; -.
DR   PhylomeDB; Q96SI9; -.
DR   TreeFam; TF320194; -.
DR   PathwayCommons; Q96SI9; -.
DR   SignaLink; Q96SI9; -.
DR   BioGRID-ORCS; 55342; 11 hits in 1159 CRISPR screens.
DR   ChiTaRS; STRBP; human.
DR   EvolutionaryTrace; Q96SI9; -.
DR   GeneWiki; STRBP; -.
DR   GenomeRNAi; 55342; -.
DR   Pharos; Q96SI9; Tbio.
DR   PRO; PR:Q96SI9; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q96SI9; Protein.
DR   Bgee; ENSG00000165209; Expressed in secondary oocyte and 185 other cell types or tissues.
DR   ExpressionAtlas; Q96SI9; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002177; C:manchette; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR   GO; GO:0048870; P:cell motility; IEA:Ensembl.
DR   GO; GO:0007638; P:mechanosensory behavior; IEA:Ensembl.
DR   GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR   CDD; cd19909; DSRM_STRBP_rpt1; 1.
DR   CDD; cd19911; DSRM_STRBP_rpt2; 1.
DR   Gene3D; 1.10.1410.40; -; 1.
DR   Gene3D; 3.30.160.20; -; 2.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR006561; DZF_dom.
DR   InterPro; IPR049402; DZF_dom_C.
DR   InterPro; IPR049401; DZF_dom_N.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR044472; STRBP_DSRM_1.
DR   PANTHER; PTHR45762:SF1; SPERMATID PERINUCLEAR RNA-BINDING PROTEIN; 1.
DR   PANTHER; PTHR45762; ZINC FINGER RNA-BINDING PROTEIN; 1.
DR   Pfam; PF00035; dsrm; 2.
DR   Pfam; PF20965; DZF_C; 1.
DR   Pfam; PF07528; DZF_N; 1.
DR   SMART; SM00358; DSRM; 2.
DR   SMART; SM00572; DZF; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR   PROSITE; PS50137; DS_RBD; 2.
DR   PROSITE; PS51703; DZF; 1.
DR   Genevisible; Q96SI9; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW   Differentiation; DNA-binding; Methylation; Reference proteome; Repeat;
KW   RNA-binding; Spermatogenesis.
FT   CHAIN           1..672
FT                   /note="Spermatid perinuclear RNA-binding protein"
FT                   /id="PRO_0000274917"
FT   DOMAIN          5..363
FT                   /note="DZF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01040"
FT   DOMAIN          387..453
FT                   /note="DRBM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT   DOMAIN          510..576
FT                   /note="DRBM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT   REGION          52..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         612
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91WM1"
FT   MOD_RES         617
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91WM1"
FT   VAR_SEQ         1..14
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11230166"
FT                   /id="VSP_022937"
FT   VARIANT         280
FT                   /note="G -> R (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035662"
FT   CONFLICT        173..175
FT                   /note="LEK -> IGRR (in Ref. 1; AAK20832)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="L -> P (in Ref. 3; BAA92120)"
FT                   /evidence="ECO:0000305"
FT   STRAND          385..387
FT                   /evidence="ECO:0007829|PDB:2DMY"
FT   HELIX           390..398
FT                   /evidence="ECO:0007829|PDB:2DMY"
FT   STRAND          405..411
FT                   /evidence="ECO:0007829|PDB:2DMY"
FT   STRAND          413..415
FT                   /evidence="ECO:0007829|PDB:2DMY"
FT   STRAND          417..424
FT                   /evidence="ECO:0007829|PDB:2DMY"
FT   STRAND          427..435
FT                   /evidence="ECO:0007829|PDB:2DMY"
FT   HELIX           436..451
FT                   /evidence="ECO:0007829|PDB:2DMY"
SQ   SEQUENCE   672 AA;  73653 MW;  26465F4D3A429FBC CRC64;
     MRSIRSFAND DRHVMVKHST IYPSPEELEA VQNMVSTVEC ALKHVSDWLD ETNKGTKTEG
     ETEVKKDEAG ENYSKDQGGR TLCGVMRIGL VAKGLLIKDD MDLELVLMCK DKPTETLLNT
     VKDNLPIQIQ KLTEEKYQVE QCVNEASIII RNTKEPTLTL KVILTSPLIR DELEKKDGEN
     VSMKDPPDLL DRQKCLNALA SLRHAKWFQA RANGLKSCVI VLRILRDLCN RVPTWAPLKG
     WPLELICEKS IGTCNRPLGA GEALRRVMEC LASGILLPGG PGLHDPCERD PTDALSYMTI
     QQKEDITHSA QHALRLSAFG QIYKVLEMDP LPSSKPFQKY SWSVTDKEGA GSSALKRPFE
     DGLGDDKDPN KKMKRNLRKI LDSKAIDLMN ALMRLNQIRP GLQYKLLSQS GPVHAPVFTM
     SVDVDGTTYE ASGPSKKTAK LHVAVKVLQA MGYPTGFDAD IECMSSDEKS DNESKNETVS
     SNSSNNTGNS TTETSSTLEV RTQGPILTAS GKNPVMELNE KRRGLKYELI SETGGSHDKR
     FVMEVEVDGQ KFRGAGPNKK VAKASAALAA LEKLFSGPNA ANNKKKKIIP QAKGVVNTAV
     SAAVQAVRGR GRGTLTRGAF VGATAAPGYI APGYGTPYGY STAAPAYGLP KRMVLLPVMK
     FPTYPVPHYS FF
//