XP2_XENLA
ID XP2_XENLA Reviewed; 439 AA.
AC P17437; Q08944;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Skin secretory protein xP2;
DE AltName: Full=Protein APEG;
DE Flags: Precursor;
GN Name=p2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-25 AND 344-439 (ISOFORM 2).
RX PubMed=1629230; DOI=10.1016/s0021-9258(19)49733-0;
RA Hauser F., Roeben C., Hoffmann W.;
RT "xP2, a new member of the P-domain peptide family of potential growth
RT factors, is synthesized in Xenopus laevis skin.";
RL J. Biol. Chem. 267:14451-14455(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-439 (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=2298293; DOI=10.1016/0014-5793(90)80088-z;
RA Gmachl M., Berger H., Thalhammer J., Kreil G.;
RT "Dermal glands of Xenopus laevis contain a polypeptide with a highly
RT repetitive amino acid sequence.";
RL FEBS Lett. 260:145-148(1990).
CC -!- FUNCTION: May act as a growth factor in the germinal layer of the
CC epidermis. May also be involved in growth of regenerating glands and in
CC protection of the skin from the external environment.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=APEG;
CC IsoId=P17437-1; Sequence=Displayed;
CC Name=2; Synonyms=XP2;
CC IsoId=P17437-2; Sequence=VSP_004652;
CC -!- TISSUE SPECIFICITY: Skin.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35759.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M90095; AAA50001.1; -; mRNA.
DR EMBL; X51394; CAA35759.1; ALT_FRAME; mRNA.
DR PIR; A37331; A37331.
DR PIR; S07498; SKXLAG.
DR AlphaFoldDB; P17437; -.
DR SMR; P17437; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR CDD; cd00111; Trefoil; 2.
DR Gene3D; 4.10.110.10; -; 2.
DR InterPro; IPR017994; P_trefoil_chordata.
DR InterPro; IPR017957; P_trefoil_CS.
DR InterPro; IPR000519; P_trefoil_dom.
DR InterPro; IPR044913; P_trefoil_dom_sf.
DR PANTHER; PTHR13826; PTHR13826; 2.
DR Pfam; PF00088; Trefoil; 2.
DR PRINTS; PR00680; PTREFOIL.
DR SMART; SM00018; PD; 2.
DR SUPFAM; SSF57492; SSF57492; 2.
DR PROSITE; PS00025; P_TREFOIL_1; 2.
DR PROSITE; PS51448; P_TREFOIL_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Growth factor; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..439
FT /note="Skin secretory protein xP2"
FT /id="PRO_0000023470"
FT REPEAT 26..33
FT /note="1"
FT REPEAT 34..41
FT /note="2"
FT REPEAT 42..51
FT /note="3"
FT REPEAT 52..59
FT /note="4"
FT REPEAT 60..69
FT /note="5"
FT REPEAT 70..77
FT /note="6; approximate"
FT REPEAT 78..87
FT /note="7"
FT REPEAT 88..97
FT /note="8"
FT REPEAT 98..107
FT /note="9"
FT REPEAT 108..115
FT /note="10"
FT REPEAT 116..125
FT /note="11"
FT REPEAT 126..135
FT /note="12"
FT REPEAT 136..145
FT /note="13"
FT REPEAT 146..153
FT /note="14"
FT REPEAT 154..163
FT /note="15"
FT REPEAT 164..173
FT /note="16; approximate"
FT REPEAT 174..183
FT /note="17"
FT REPEAT 184..193
FT /note="18"
FT REPEAT 194..203
FT /note="19"
FT REPEAT 204..215
FT /note="20"
FT REPEAT 216..225
FT /note="21"
FT REPEAT 226..235
FT /note="22"
FT REPEAT 236..245
FT /note="23"
FT REPEAT 246..255
FT /note="24"
FT REPEAT 256..265
FT /note="25"
FT REPEAT 266..275
FT /note="26"
FT REPEAT 276..285
FT /note="27"
FT REPEAT 286..293
FT /note="28"
FT REPEAT 294..303
FT /note="29"
FT REPEAT 304..313
FT /note="30"
FT REPEAT 314..321
FT /note="31; approximate"
FT REPEAT 322..331
FT /note="32; approximate"
FT REPEAT 332..343
FT /note="33; approximate"
FT DOMAIN 349..392
FT /note="P-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DOMAIN 396..439
FT /note="P-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT REGION 25..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..343
FT /note="33 X approximate repeats of G-G(0,1)-[EV](0,1)-A-P-
FT [A-P](1,3)-A-E"
FT COMPBIAS 86..100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..278
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 351..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 361..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 371..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 398..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 408..423
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT DISULFID 418..435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00779"
FT VAR_SEQ 26..343
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1629230"
FT /id="VSP_004652"
FT CONFLICT 3
FT /note="H -> S (in Ref. 2; CAA35759)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="C -> W (in Ref. 2; CAA35759)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 41173 MW; 38C4A4B57CBAE778 CRC64;
MNHKLFCVHF LLLILSVCYI QGQDAGGEPA PAEGVAPAPA EGGAPAPAPA EGEAPAPAEG
GAPAPAPAEG AEPAPADGGA PAPAPAEGGA PAPAPAEGGA PAPAPAEGGA PAPAEGGAPA
PAPAEGEAPA PAPAEGEAPA PAPAEGEAPA PAEGEAPAPA PAEVEAPAPA PAEGEAPAPA
PAEGEAPAPA PAEGEAPAPA PAEGEAPAPA PAPAEGEAPA PAPAEGEAPA PAPAEGEAPA
PAPAEGEAPA PAPAEGEAPA PAPAEGEAPA PAPAEGEAPA PAPAEGEAPA PAEGEAPAPA
PAEGEAPAPA PAEGGAPSPA EGGAPAAAPA EGGAPAPAPA PVEVGPKTED CKGDPFKRTD
CGYPGITEGQ CKAKGCCFDS SIVGVKWCFF PRTARAQCLF SPGDREDCGY SSITPMECMK
RGCCFDASIT GVKWCFHQK
