new test file

new test file

git-svn-id: ed25c26de1c5325e8eb0deed0b990ab8af8a4def@3047 7c6358e6-4a41-0410-a743-a5b2a554c398

ID   AAC4_HUMAN     STANDARD;      PRT;   911 AA.
AC   O43707; O76048;
DT   16-OCT-2001 (Rel. 40, Created)
DT   16-OCT-2001 (Rel. 40, Last sequence update)
DT   10-OCT-2003 (Rel. 42, Last annotation update)
DE   Alpha-actinin 4 (Non-muscle alpha-actinin 4) (F-actin cross linking
DE   protein).
GN   ACTN4.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE OF 4-911 FROM N.A.
RX   MEDLINE=98177166; PubMed=9508771;
RA   Honda K., Yamada T., Endo R., Ino Y., Gotoh M., Tsuda H., Yamada Y.,
RA   Chiba H., Hirohashi S.;
RT   "Actinin-4, a novel actin-bundling protein associated with cell
RT   motility and cancer invasion.";
RL   J. Cell Biol. 140:1383-1393(1998).
RN   [2]
RP   ERRATUM.
RA   Honda K., Yamada T., Endo R., Ino Y., Gotoh M., Tsuda H., Yamada Y.,
RA   Chiba H., Hirohashi S.;
RL   J. Cell Biol. 143:276-276(1998).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   TISSUE=Neuroblastoma;
RX   MEDLINE=20120478; PubMed=10656685;
RA   Nikolopoulos S.N., Spengler B.A., Kisselbach K., Evans A.E.,
RA   Biedler J.L., Ross R.A.;
RT   "The human non-muscle alpha-actinin protein encoded by the ACTN4 gene
RT   suppresses tumorigenicity of human neuroblastoma cells.";
RL   Oncogene 19:380-386(2000).
RN   [4]
RP   SEQUENCE FROM N.A.
RC   TISSUE=Placenta;
RX   MEDLINE=22388257; PubMed=12477932;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length
RT   human and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN   [5]
RP   SEQUENCE OF 1-170 FROM N.A.
RA   Ottenwaelder B., Obermaier B., Mewes H.-W., Gassenhuber J.,
RA   Wiemann S.;
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   SEQUENCE OF 1-218 FROM N.A.
RA   Isogai T., Otsuki T., Sugiyama T.;
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   VARIANTS FSGS1 GLU-255; ILE-259 AND PRO-262.
RC   TISSUE=Lymphocytes;
RX   MEDLINE=20164321; PubMed=10700177;
RA   Kaplan J.M., Kim S.H., North K.N., Rennke H., Correia L.A.,
RA   Tong H.-Q., Mathis B.J., Rodriguez-Perez J.-C., Allen P.G.,
RA   Beggs A.H., Pollak M.R.;
RT   "Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal
RT   segmental glomerulosclerosis.";
RL   Nat. Genet. 24:251-256(2000).
CC   -!- FUNCTION: F-ACTIN CROSS-LINKING PROTEIN WHICH IS THOUGHT TO ANCHOR
CC       ACTIN TO A VARIETY OF INTRACELLULAR STRUCTURES. THIS IS A BUNDLING
CC       PROTEIN.
CC   -!- SUBUNIT: HOMODIMER, ANTIPARALLEL (BY SIMILARITY).
CC   -!- SUBCELLULAR LOCATION: NUCLEAR AND CYTOPLASMIC. COLOCALIZES WITH
CC       ACTIN STRESS FIBERS. NUCLEAR TRANSLOCATION CAN BE INDUCED BY THE
CC       PI3 KINASE INHIBITOR WORTMANNIN OR BY CYTOCHALASIN D. EXCLUSIVELY
CC       LOCALIZED IN THE NUCLEUS IN A LIMITED NUMBER OF CELL LINES (BREAST
CC       CANCER CELL LINE MCF7, ORAL FLOOR CANCER IMC2, AND BLADDER CANCER
CC       KU7).
CC   -!- TISSUE SPECIFICITY: WIDELY EXPRESSED.
CC   -!- DISEASE: CYTOPLASMIC LOCALIZATION OF ACTN4 MAY BE ASSOCIATED WITH
CC       CANCER METASTASES DUE TO ENHANCED CELL MOTILITY.
CC   -!- DISEASE: DEFECTS IN ACTN4 ARE THE CAUSE OF FOCAL SEGMENTAL
CC       GLOMERULOSCLEROSIS 1 (FSGS1) [MIM:603278], A COMMON RENAL LESION
CC       CHARACTERIZED BY INCREASED URINARY PROTEIN EXCRETION AND
CC       DECREASING KIDNEY FUNCTION. RENAL INSUFFICIENCY OFTEN PROGRESSES
CC       TO END-STAGE RENAL FAILURE, A HIGHLY MORBID STATE REQUIRING EITHER
CC       DIALYSIS THERAPY OR KIDNEY TRANSPLANTATION. FSGS IS DEFINED BY THE
CC       PRESENCE OF SEGMENTAL SCLEROSIS IN GLOMERULI, AND IS SEEN IN ALL
CC       ETHNIC GROUPS, ALTHOUGH IT IS PARTICULARLY COMMON IN INDIVIDUALS
CC       OF AFRICAN DESCENT. FSGS OCCURS AS AN ISOLATED PRIMARY CONDITION
CC       OR SECONDARY TO DISORDERS AS HIV INFECTION, OBESITY, HYPERTENSION
CC       AND DIABETES. FSGS MAY ALSO BE INHERITED AS A MENDELIAN TRAIT.
CC   -!- SIMILARITY: CONTAINS 1 ACTIN-BINDING DOMAIN.
CC   -!- SIMILARITY: CONTAINS 2 CALPONIN-HOMOLOGY (CH) DOMAINS.
CC   -!- SIMILARITY: CONTAINS 2 EF-HAND CALCIUM-BINDING DOMAINS.
CC   -!- SIMILARITY: CONTAINS 4 SPECTRIN REPEATS.
CC   -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN BY A HIGH NUMBER
CC       OF FRAMESHIFTS, SOME OF WHICH WE HAVE CORRECTED. THE REMAINING
CC       SEQUENCE CONFLICTS INCLUDE BOTH SMALL FRAMESHIFTS AS WELL AS POINT
CC       CHANGES. THEY ARE PROBABLY SEQUENCING ERRORS WHEN COMPARED WITH
CC       THE OTHER MAMMALIAN SEQUENCES.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; D89980; BAA24447.1; ALT_INIT.
DR   EMBL; U48734; AAC17470.1; ALT_FRAME.
DR   EMBL; BC005033; AAH05033.1; -.
DR   EMBL; AL047603; -; NOT_ANNOTATED_CDS.
DR   EMBL; AU118403; -; NOT_ANNOTATED_CDS.
DR   HSSP; Q01082; 1BKR.
DR   Genew; HGNC:166; ACTN4.
DR   MIM; 604638; -.
DR   MIM; 603278; -.
DR   GO; GO:0015629; C:actin cytoskeleton; TAS.
DR   GO; GO:0005737; C:cytoplasm; TAS.
DR   GO; GO:0005634; C:nucleus; TAS.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; TAS.
DR   GO; GO:0006928; P:cell motility; TAS.
DR   GO; GO:0007125; P:invasive growth; TAS.
DR   InterPro; IPR001589; Actbind_actnin.
DR   InterPro; IPR001715; Calponin-like.
DR   InterPro; IPR002048; EF-hand.
DR   InterPro; IPR002017; Spectrin.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF00036; efhand; 2.
DR   Pfam; PF00435; spectrin; 4.
DR   ProDom; PD000012; EF-hand; 1.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00150; SPEC; 3.
DR   PROSITE; PS00018; EF_HAND; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
KW   Actin-binding; Calcium-binding; Repeat; Multigene family;
KW   Disease mutation; Nuclear protein.
FT   DOMAIN        1    269       ACTIN-BINDING (BY SIMILARITY).
FT   DOMAIN       50    154       CH 1.
FT   DOMAIN      163    269       CH 2.
FT   DOMAIN      177    192       POLYPHOSPHOINOSITIDE (PIP2)-BINDING
FT                                (POTENTIAL).
FT   REPEAT      293    403       SPECTRIN 1.
FT   REPEAT      413    518       SPECTRIN 2.
FT   REPEAT      528    639       SPECTRIN 3.
FT   REPEAT      649    752       SPECTRIN 4.
FT   CA_BIND     778    789       EF-HAND 1 (POTENTIAL).
FT   CA_BIND     819    830       EF-HAND 2 (POTENTIAL).
FT   DOMAIN       19     26       POLY-GLY.
FT   VARIANT     255    255       K -> E (in FSGS1).
FT                                /FTId=VAR_010378.
FT   VARIANT     259    259       T -> I (in FSGS1).
FT                                /FTId=VAR_010379.
FT   VARIANT     262    262       S -> P (in FSGS1).
FT                                /FTId=VAR_010380.
FT   CONFLICT     60     60       C -> S (IN REF. 3).
FT   CONFLICT    124    124       V -> I (IN REF. 3).
FT   CONFLICT    164    164       S -> L (IN REF. 4).
FT   CONFLICT    276    276       T -> TET (IN REF. 3).
FT   CONFLICT    292    294       EHL -> CSTS (IN REF. 3).
FT   CONFLICT    359    360       TL -> SV (IN REF. 3).
FT   CONFLICT    476    476       I -> S (IN REF. 3).
FT   CONFLICT    526    526       I -> II (IN REF. 3).
FT   CONFLICT    536    536       R -> P (IN REF. 3).
FT   CONFLICT    645    645       Q -> QQ (IN REF. 3).
FT   CONFLICT    673    674       GR -> A (IN REF. 3).
FT   CONFLICT    850    850       A -> T (IN REF. 3).
FT   CONFLICT    859    859       MISSING (IN REF. 3).
FT   CONFLICT    891    893       AVP -> GVR (IN REF. 3).
SQ   SEQUENCE   911 AA;  104854 MW;  461580C3F22937D1 CRC64;
     MVDYHAANQS YQYGPSSAGN GAGGGGSMGD YMAQEDDWDR DLLLDPAWEK QQRKTFTAWC
     NSHLRKAGTQ IENIDEDFRD GLKLMLLLEV ISGERLPKPE RGKMRVHKIN NVNKALDFIA
     SKGVKLVSIG AEEIVDGNAK MTLGMIWTII LRFAIQDISV EETSAKEGLL LWCQRKTAPY
     KNVNVQNFHI SWKDGLAFNA LIHRHRPELI EYDKLRKDDP VTNLNNAFEV AEKYLDIPKM
     LDAEDIVNTA RPDEKAIMTY VSSFYHAFSG AQKAETAANR ICKVLAVNQE NEHLMEDYEK
     LASDLLEWIR RTIPWLEDRV PQKTIQEMQQ KLEDFRDYRR VHKPPKVQEK CQLEINFNTL
     QTKLRLSNRP AFMPSEGKMV SDINNGWQHL EQAEKGYEEW LLNEIRRLER LDHLAEKFRQ
     KASIHEAWTD GKEAMLKHRD YETATLSDIK ALIRKHEAFE SDLAAHQDRV EQIAAIAQEL
     NELDYYDSHN VNTRCQKICD QWDALGSLTH SRREALEKTE KQLEAIDQLH LEYAKRAAPF
     NNWMESAMED LQDMFIVHTI EEIEGLISAH DQFKSTLPDA DREREAILAI HKEAQRIAES
     NHIKLSGSNP YTTVTPQIIN SKWEKVQQLV PKRDHALLEE QSKQQSNEHL RRQFASQANV
     VGPWIQTKME EIGRISIEMN GTLEDQLSHL KQYERSIVDY KPNLDLLEQQ HQLIQEALIF
     DNKHTNYTME HIRVGWEQLL TTIARTINEV ENQILTRDAK GISQEQMQEF RASFNHFDKD
     HGGALGPEEF KACLISLGYD VENDRQGEAE FNRIMSLVDP NHSGLVTFQA FIDFMSRETT
     DTDTADQVIA SFKVLAGDKN FITAEELRRE LPPDQAEYCI ARMAPYQGPD AVPGALDYKS
     FSTALYGESD L
//

error: pathspec 'tests/files/AAC4_HUMAN.sp' did not match any file(s) known to git


added missing file

added missing file

'imp' 'imp.wav' loadfile
'seq' '60 62 64 66 67 69 72' gen_vals

110 '+2(++)--' prop dup
1 'seq' tseq mtof
0.4 48 mtof pluck dup

1024 'imp' conv  0.03 * +

error: pathspec 'examples/conv.sp' did not match any file(s) known to git


With newest soundpipe, you don't want ampdb here

2.5 metro
200
500 trand
0.1 saw

20 1024 ptrack sine

2.5 metro
200
500 trand
0.1 saw

20 1024 ptrack ampdb sine


Cleanup some tag mismatch errors

Cleanup some tag mismatch errors

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